This review presents a general view of all types of melanin in all types of organisms. Melanin is frequently considered just an animal cutaneous pigment and is treated separately from similar fungal or bacterial pigments. Similarities concerning the phenol precursors and common patterns in the formation routes are discussed. All melanins are formed in a first enzymatically-controlled phase, generally a phenolase, and a second phase characterized by an uncontrolled polymerization of the oxidized intermediates. In that second phase, quinones derived from phenol oxidation play a crucial role. Concerning functions, all melanins show a common feature, a protective role, but they are not merely photoprotective pigments against UV sunlight. In pathogenic microorganisms, melanization becomes a virulence factor since melanin protects microbial cells from defense mechanisms in the infected host. In turn, some melanins are formed in tissues where sunlight radiation is not a potential threat. Then, their redox, metal chelating, or free radical scavenging properties are more important than light absorption capacity. These pigments sometimes behave as a double-edged sword, and inhibition of melanogenesis is desirable in different cells. Melanin biochemistry is an active field of research from dermatological, biomedical, cosmetical, and microbiological points of view, as well as fruit technology. 1. Antecedents, Concept, Types, and Occurrence Melanin is the generic name used to refer to perhaps the most ubiquitous, resistant, heterogeneous, and ancient pigments found in nature. Melanin appeared very early in most living kingdoms on the Earth. Thus, melanin has been recently found in very old fossils from dinosaurs, early birds, nonavian theropod species [1, 2], and primitive cephalopods [3]. These recent findings will probably make melanin a new biomarker in life evolution. The name “melanin” comes from the ancient Greek melanos, meaning “dark,” and, according to Borovansky [4], the term was probably first applied by the Swedish chemist Berzelius in 1840 to call a dark pigment extracted from eye membranes [5]. However, first references of human skin pigmentation and somehow to the existence of melanin without using the current name are very old. Pharaonic medicine in the Ebers Papyrus (1550 BC) described some diseases affecting skin color [6], and one of them was probably vitiligo, although that term appeared much later, derived from the Latin word “vitellus” meaning “veal” or pale pink skin [7]. The first relatively detailed written description on skin pigmentation
References
[1]
F. Zhang, S. L. Kearns, P. J. Orr et al., “Fossilized melanosomes and the colour of Cretaceous dinosaurs and birds,” Nature, vol. 463, no. 7284, pp. 1075–1078, 2010.
[2]
R. A. Wogelius, P. L. Manning, H. E. Barden et al., “Trace metals as biomarkers for eumelanin pigment in the fossil record,” Science, vol. 333, no. 6049, pp. 1622–1626, 2011.
[3]
K. Glass, S. Ito, P. R. Wilby, et al., “Direct chemical evidence for undegraded eumelanin pigment from the jurassic period,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, pp. 10218–10223, 2012.
[4]
J. Borovansky, “History of melanosome research,” in Melanins and Melanosomes: Biosynthesis, Biogenesis, Physiological, and Pathological Functions, J. Borovansky and P. A. Riley, Eds., pp. 1–19, Wiley-VCH Verlag GmbH & Co. KGaA, 1st edition, 2011.
[5]
J. J. Berzelius, Lehrbuch der Chemie, vol. 9, 1840.
[6]
B. Ebbell, the Papyrus Ebers. the Greatest Egyptian Medical Document, Levin and Munksgaard, Copenhagen, Denmark, 1937.
[7]
W. Westerhof, “The discovery of the human melanocyte,” Pigment Cell Research, vol. 19, no. 3, pp. 183–193, 2006.
[8]
R. A. Nicolaus, Melanins, Chemistry of Natural Products Series, Hermann, Paris, Edited by E. Lederer, 1968.
[9]
G. Prota, Melanins and Melanogenesis, Academic Press, San Diego, Calif, USA, 1992.
[10]
M. d’Ischia, K. Wakamatsu, A. Napolitano, et al., “Melanins and melanogenesis: methods, standards, protocols,” Pigment Cell and Melanoma Research, vol. 26, no. 5, pp. 616–633, 2013.
[11]
N. Jablonsky, Skin: A Natural History, University of California Press, Berkeley, Calif, USA, 2006.
[12]
W. C. Quevedo Jr., T. B. Fitzpatrick, and K. Jimbow, “Human skin color: origin, variation and significance,” Journal of Human Evolution, vol. 14, no. 1, pp. 43–56, 1985.
[13]
J. Y. Lin and D. E. Fisher, “Melanocyte biology and skin pigmentation,” Nature, vol. 445, no. 7130, pp. 843–850, 2007.
[14]
P. Sulem, D. F. Gudbjartsson, S. N. Stacey et al., “Genetic determinants of hair, eye and skin pigmentation in Europeans,” Nature Genetics, vol. 39, no. 12, pp. 1443–1452, 2007.
[15]
R. A. Sturm, “Molecular genetics of human pigmentation diversity,” Human Molecular Genetics, vol. 18, no. 1, pp. R9–R17, 2009.
[16]
G. Britton, “Structure and properties of carotenoids in relation to function,” The FASEB Journal, vol. 9, no. 15, pp. 1551–1558, 1995.
[17]
M. Richelle, M. Sabatier, H. Steiling, and G. Williamson, “Skin bioavailability of dietary vitamin E, carotenoids, polyphenols, vitamin C, zinc and selenium,” British Journal of Nutrition, vol. 96, no. 2, pp. 227–238, 2006.
[18]
N. Samson, B. Fink, and P. J. Matts, “Visible skin condition and perception of human facial appearance,” International Journal of Cosmetic Science, vol. 32, no. 3, pp. 167–184, 2010.
[19]
J. D. Simon and D. N. Peles, “The red and the black,” Accounts of Chemical Research, vol. 43, no. 11, pp. 1452–1460, 2010.
[20]
R. Robbins, “Chemical and physical behavior of human hair,” in Genetic Control/Involvement in Hair Fiber Traits, chapter 3, pp. 177–203, Springer, Berlin, Germany, 5th edition, 2012.
[21]
B. B. Adhyaru, N. G. Akhmedov, A. R. Katritzky, and C. R. Bowers, “Solid-state cross-polarization magic angle spinning 13C and 15N NMR characterization of Sepia melanin, Sepia melanin free acid and Human hair melanin in comparison with several model compounds,” Magnetic Resonance in Chemistry, vol. 41, no. 6, pp. 466–474, 2003.
[22]
P. Thureau, F. Ziarelli, A. Thévand, et al., “Probing the motional behavior of eumelanin and pheomelanin with solid-state NMR spectroscopy: new insights into the pigment properties,” Chemistry, vol. 18, no. 34, pp. 10689–10700, 2012.
[23]
S. Ghiani, S. Baroni, D. Burgio et al., “Characterization of human hair melanin and its degradation products by means of magnetic resonance techniques,” Magnetic Resonance in Chemistry, vol. 46, no. 5, pp. 471–479, 2008.
[24]
S. Ito and K. Fujita, “Microanalysis of eumelanin and pheomelanin in hair and melanomas by chemical degradation and liquid chromatography,” Analytical Biochemistry, vol. 144, no. 2, pp. 527–536, 1985.
[25]
S. Ito, “Reexamination of the structure of eumelanin,” Biochimica et Biophysica Acta, vol. 883, no. 1, pp. 155–161, 1986.
[26]
S. Ito and K. Wakamatsu, “Quantitative analysis of eumelanin and pheomelanin in humans, mice, and other animals: a comparative review,” Pigment Cell Research, vol. 16, no. 5, pp. 523–531, 2003.
[27]
S. Ito, K. Wakamatsu, K. Glass, and J. D. Simon, “High-performance liquid chromatography estimation of cross-linking of dihydroxyindole moiety in eumelanin,” Analytical Biochemistry, vol. 434, pp. 221–225, 2013.
[28]
J. D. Simon, D. Peles, K. Wakamatsu, and S. Ito, “Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology, and function,” Pigment Cell and Melanoma Research, vol. 22, no. 5, pp. 563–579, 2009.
[29]
H. S. Mason, “The chemistry of melanin. Mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase,” The Journal of Biological Chemistry, vol. 172, pp. 83–99, 1948.
[30]
Empirical formulae for eumelanin, http://www.chemspider.com/Chemical-Structure.4884931.html.
[31]
A. J. Nappi and M. Sugumaran, “Some biochemical aspects of eumelanin formation in insect immunity,” in Insect Immunity, J. P. N. Pathak, Ed., chapter 10, pp. 131–138, Kluwer Academic Publishers, New Delhi, India, 1993.
[32]
G. Prota, “Recent advances in the chemistry of melanogenesis in mammals,” Journal of Investigative Dermatology, vol. 75, no. 1, pp. 122–127, 1980.
[33]
G. Prota, “Progress in the chemistry of melanins and related metabolites,” Medicinal Research Reviews, vol. 8, no. 4, pp. 525–556, 1988.
[34]
A. Palumbo, F. Solano, G. Misuraca et al., “Comparative action of dopachrome tautomerase and metal ions on the rearrangement of dopachrome,” Biochimica et Biophysica Acta–General Subjects, vol. 1115, no. 1, pp. 1–5, 1991.
[35]
P. Aroca, F. Solano, C. Salinas, J. C. Garcia-Borron, and J. A. Lozano, “Regulation of the final phase of mammalian melanogenesis. The role of dopachrome tautomerase and the ratio between 5,6-dihydroxyindole-2-carboxylic acid and 5,6-dihydroxyindole,” European Journal of Biochemistry, vol. 208, no. 1, pp. 155–163, 1992.
[36]
S. Ito and K. Wakamatsu, “Chemistry of mixed melanogenesis–pivotal roles of dopaquinone,” Photochemistry and Photobiology, vol. 84, no. 3, pp. 582–592, 2008.
[37]
J. C. García-Borrón, M. D. Saura, F. Solano, J. L. Iborra, and J. A. Lozano, “FT-IR spectroscopy of natural melanins isolated from Harding-Passey mouse melanoma,” Physiological Chemistry and Physics and Medical NMR, vol. 17, no. 2, pp. 211–218, 1985.
[38]
M. Piattelli, E. Fattorusso, S. Magno, and R. A. Nicolaus, “The structure of melanins and melanogenesis-III. The structure of sepiomelanin,” Tetrahedron, vol. 19, no. 12, pp. 2061–2072, 1963.
[39]
H. S. Mason and E. W. Peterson, “Melanoproteins I. Reactions between enzyme-generated quinones and amino acids,” Biochimica et Biophysica Acta, vol. 111, no. 1, pp. 134–146, 1965.
[40]
C. Salinas, J. C. Garcia-Borron, F. Solano, and J. A. Lozano, “Dopachrome tautomerase decreases the binding of indolic melanogenesis intermediates to proteins,” Biochimica et Biophysica Acta, vol. 1204, no. 1, pp. 53–60, 1994.
[41]
A. Palumbo, M. D'Ischia, G. Misuraca, A. Iannone, and G. Prota, “Selective uptake of 2-thiouracil into melanin-producing systems depends on chemical binding to enzymically generated dopaquinone,” Biochimica et Biophysica Acta, vol. 1036, no. 3, pp. 221–227, 1990.
[42]
A. Palumbo, A. Napolitano, L. de Martino, W. Vieira, and V. J. Hearing, “Specific incorporation of 2-thiouracil into biological melanins,” Biochimica et Biophysica Acta, vol. 1200, no. 3, pp. 271–276, 1994.
[43]
G. Prota and R. H. Thomson, “Melanin pigmentation in mammals,” Endeavour, vol. 35, no. 124, pp. 32–38, 1976.
[44]
H. Rorsman, G. Agrup, C. Hansson, A. M. Rosengren, and E. Rosengren, “Detection of pheomelanins,” in Pigment Cell, vol. 4, pp. 244–252, S. Karger, Basel, Switzerland, Edited by by S. N. Klaus, 1979.
[45]
G. Prota and R. A. Nicolaus, “On the biogenesis of phaeomelanins,” in The Pigmentary System, Advances in Biology of Skin, W. Montagna and F. Flu, Eds., vol. 8, pp. 323–328, Pergamon Press, New York, NY, USA, 1967.
[46]
S. Ito, K. Fujita, M. Yoshioka, D. Sienko, and T. Nagatsu, “Identification of 5-S and 2-S-cysteinyldopamine and 5-S-glutathionyldopamine formed from dopamine by high-performance liquid chromatography with electrochemical detection,” Journal of Chromatography—Biomedical Applications, vol. 375, no. 1, pp. 134–140, 1986.
[47]
G. G. Panzella, L. Verotta, M. d'Ischia, and A. Napolitano, “Uncovering the structure of human red hair pheomelanin: benzothiazolylthiazinodihydroisoquinolines as key building blocks,” Journal of Natural Products, vol. 74, no. 4, pp. 675–682, 2011.
[48]
A. Napolitano, L. Panzella, and L. Leone M d’Ischia, “Red hair benzothiazines and benzothiazoles: mutation-inspired chemistry in the quest for functionality,” Accounts of Chemical Research, vol. 46, no. 2, pp. 519–528, 2013.
[49]
K. Wakamatsu, K. Ohtara, and S. Ito, “Chemical analysis of late stages of pheomelanogenesis: conversion of dihydrobenzothiazine to a benzothiazole structure,” Pigment Cell and Melanoma Research, vol. 22, no. 4, pp. 474–486, 2009.
[50]
A. Roulin, K. Mafli, and K. Wakamatsu, “Reptiles produce pheomelanin: evidence in the eastern Hermann's tortoise (Eurotestudo boettgeri),” Journal of Herpetology, vol. 47, no. 2, pp. 258–261, 2013.
[51]
B. E. Ivine and R. K. Holmes, “Factors affecting phaeomelanin production by a melanin-producing (mel) mutant of Vibrio cholerae,” Infection and Immunity, vol. 34, no. 3, pp. 895–899, 1981.
[52]
M. Ye, X. Chen, G. Li, G. Guo, and L. Yang, “Structural characteristics of pheomelanin-like pigment from lachnum singerianum,” Advanced Materials Research, vol. 284–286, pp. 1742–1745, 2011.
[53]
W. D. Bush, J. Garguilo, F. A. Zucca et al., “The surface oxidation potential of human neuromelanin reveals a spherical architecture with a pheomelanin core and a eumelanin surface,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 40, pp. 14785–14789, 2006.
[54]
A. S. Breathnach, “Extra-cutaneous melanin,” Pigment Cell Research, vol. 1, no. 4, pp. 234–237, 1988.
[55]
J. J. Weiter, F. C. Delori, G. L. Wing, and K. A. Fitch, “Retinal pigment epithelial lipofuscin and melanin and choroidal melanin in human eyes,” Investigative Ophthalmology and Visual Science, vol. 27, no. 2, pp. 145–152, 1986.
[56]
U. Schraermeyer and K. Heimann, “Current understanding on the role of retinal pigment epithelium and its pigmentation,” Pigment Cell Research, vol. 12, no. 4, pp. 219–236, 1999.
[57]
A. M. Meyer zum Gottesberge-Orsulakova, “Melanin in the inner ear: micromorphological and microanalytical investigations,” Acta Histochemica. Supplementband, vol. 32, pp. 245–253, 1986.
[58]
S. Murillo-Cuesta, J. Contreras, E. Zurita et al., “Melanin precursors prevent premature age-related and noise-induced hearing loss in albino mice,” Pigment Cell and Melanoma Research, vol. 23, no. 1, pp. 72–83, 2010.
[59]
D. G. Graham, “On the origin and significance of neuromelanin,” Archives of Pathology and Laboratory Medicine, vol. 103, no. 7, pp. 359–362, 1979.
[60]
H. Fedorow, F. Tribl, G. Halliday, M. Gerlach, P. Riederer, and K. L. Double, “Neuromelanin in human dopamine neurons: comparison with peripheral melanins and relevance to Parkinson's disease,” Progress in Neurobiology, vol. 75, no. 2, pp. 109–124, 2005.
[61]
R. Carstam, C. Brinck, A. Hindemith-Augustsson, H. Rorsman, and E. Rosengren, “The neuromelanin of the human substantia nigra,” Biochimica et Biophysica Acta, vol. 1097, no. 2, pp. 152–160, 1991.
[62]
G. Odh, R. Carstam, J. Paulson, A. Wittbjer, E. Rosengren, and H. Rorsman, “Neuromelanin of the human substantia nigra: a mixed-type melanin,” Journal of Neurochemistry, vol. 62, no. 5, pp. 2030–2036, 1994.
[63]
F. Solano, V. J. Hearing, and J. C. Garcia-Borron, “Neurotoxicity due to o-quinones: neuromelanin formation and possible mechanisms for o-quinone detoxification,” Neurotoxicity Research, vol. 1, pp. 153–169, 2000.
[64]
L. Zecca, D. Tampellini, M. Gerlach, P. Riederer, R. G. Fariello, and D. Sulzer, “Substantia nigra neuromelanin: structure, synthesis, and molecular behaviour,” Journal of Clinical Pathology—Molecular Pathology, vol. 54, no. 6, pp. 414–418, 2001.
[65]
K. Wakamatsu, K. Fujikawa, F. A. Zucca, L. Zecca, and S. Ito, “The structure of neuromelanin as studied by chemical degradative methods,” Journal of Neurochemistry, vol. 86, no. 4, pp. 1015–1023, 2003.
[66]
K. L. Double and G. M. Halliday, “New face of neuromelanin,” Journal of Neural Transmission, Supplement, no. 70, pp. 119–123, 2006.
[67]
M. M. Piotr, A. Proszowska, A. Bucinski, and R. Kaliszan, “Affinity chromatography method for determination of binding of drugs to melanin and evaluation of side effect potential of antipsychotic agents,” Current Pharmaceutical Analysis, vol. 9, no. 2, pp. 131–138, 2013.
[68]
M. B. H. Youdim, D. Ben-Shachar, and P. Riederer, “The enigma of neuromelanin in Parkinson's disease substantia nigra,” Journal of Neural Transmission, Supplement, no. 43, pp. 113–122, 1994.
[69]
M. Randhawa, T. Huff, J. C. Valencia et al., “Evidence for the ectopic synthesis of melanin in human adipose tissue,” The FASEB Journal, vol. 23, no. 3, pp. 835–843, 2009.
[70]
S. Page, V. Chandhoke, and A. Baranova, “Melanin and melanogenesis in adipose tissue: possible mechanisms for abating oxidative stress and inflammation?” Obesity Reviews, vol. 12, no. 5, pp. e21–e31, 2011.
[71]
K. J. McGraw, K. Wakamatsu, S. Ito et al., “You can't judge a pigment by its color: carotenoid and melanin content of yellow and brown feathers in swallows, bluebirds, penguins, and domestic chickens,” The Condor, vol. 106, no. 2, pp. 390–395, 2004.
[72]
J. A. Brumbaugh, “Ultrastructural differences between forming eumelanin and pheomelanin as revealed by the pink-eye mutation in the fowl,” Developmental Biology, vol. 18, no. 4, pp. 375–390, 1968.
[73]
K. J. McGraw, R. J. Safran, and K. Wakamatsu, “How feather colour reflects its melanin content,” Functional Ecology, vol. 19, no. 5, pp. 816–821, 2005.
[74]
I. Galván and F. Solano, “The evolution of eu- and pheomelanic traits may respond to an economy of pigments related to environmental oxidative stress,” Pigment Cell and Melanoma Research, vol. 22, no. 3, pp. 339–342, 2009.
[75]
B. Almasi, L. Jenni, S. Jenni-Eiermann, and A. Roulin, “Regulation of stress response is heritable and functionally linked to melanin-based coloration,” Journal of Evolutionary Biology, vol. 23, no. 5, pp. 987–996, 2010.
[76]
M. E. Hadley and J. M. Goldman, “Physiological color changes in reptiles,” American Zoologist, vol. 9, no. 2, pp. 489–504, 1969.
[77]
B. I. Baker, “The role of melanin-concentrating hormone in color change,” Annals of the New York Academy of Sciences, vol. 680, pp. 279–289, 1993.
[78]
H. P. Wassermann, “Leukocytes and melanin pigmentation. Demonstration of pigmented leukocytes in blood of amphibians, reptiles and normal man,” The Journal of Investigative Dermatology, vol. 45, pp. 104–109, 1965.
[79]
M. Scalia, E. Geremia, C. Corsaro, C. Santoro, S. Sciuto, and G. Sichel, “The extracutaneous pigmentary system: evidence for the melanosynthesis in Amphibia and Reptilia liver,” Comparative Biochemistry and Physiology B, vol. 89, no. 4, pp. 715–717, 1988.
[80]
A. Zuasti, J. R. Jara, C. Ferrer, and F. Solano, “Occurrence of melanin granules and melanosynthesis in the kidney of Sparus auratus,” Pigment Cell Research, vol. 2, no. 2, pp. 93–99, 1989.
[81]
A. Zuasti, C. Ferrer, P. Aroca, and F. Solano, “Distribution of extracutaneous melanin pigment in Sparus auratus, Mugil cephalus, and Dicertranchus labrax (Pisces, Teleostei),” Pigment Cell Research, vol. 3, no. 3, pp. 126–131, 1990.
[82]
A. Pezzella, M. D'Ischia, A. Napolitano, A. Palumbo, and G. Prota, “An integrated approach to the structure of sepia melanin. Evidence for a high proportion of degraded 5,6-Dihydroxyindole-2-carboxylic acid units in the pigment backbone,” Tetrahedron, vol. 53, no. 24, pp. 8281–8286, 1997.
[83]
R. C. Sealy, “Free radicals in melanin Formation, Structure and reactions,” in Free Radicals in Molecular Biology, Aging and Disease, D. Armstrong, Ed., pp. 67–76, Raven Press, New York, NY, USA, 1984.
[84]
V. B. Wigglesworth, “The insect cuticle,” Biological Reviews of the Cambridge Philosophical Society, vol. 23, no. 4, pp. 408–451, 1948.
[85]
M. Sugumaran, “Molecular mechanisms for mammalian melanogenesis. Comparison with insect cuticular sclerotization,” FEBS Letters, vol. 293, no. 1, pp. 4–10, 1991.
[86]
M. Sugumaran, “Unified mechanism for sclerotization of insect cuticle,” Advances in Insect Physiology, vol. 27, pp. 229–334, 1998.
[87]
M. Sugumaran, “Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects,” Pigment Cell Research, vol. 15, no. 1, pp. 2–9, 2002.
[88]
J. R. True, “Insect melanism: the molecules matter,” Trends in Ecology and Evolution, vol. 18, no. 12, pp. 640–647, 2003.
[89]
I. M. Dubovskiy, M. M. A. Whitten, V. Y. Kryukov, et al., “More than a colour change: insect melanism, disease resistance and fecundity,” Proceeding of Royal Society B, vol. 280, no. 1763, Article ID 20130584, 2013.
[90]
P. E. Dunn, “Biochemical aspects of insect immunology,” Annual Review of Entomology, vol. 31, pp. 321–339, 1986.
[91]
A. J. Nappi and B. M. Christensen, “Melanogenesis and associated cytotoxic reactions: applications to insect innate immunity,” Insect Biochemistry and Molecular Biology, vol. 35, no. 5, pp. 443–459, 2005.
[92]
I. Eleftherianos and C. Revenis, “Role and importance of phenoloxidase in insect hemostasis,” Journal of Innate Immunity, vol. 3, no. 1, pp. 28–33, 2011.
[93]
A. M. Mayer, “Polyphenol oxidases in plants-recent progress,” Phytochemistry, vol. 26, no. 1, pp. 11–20, 1986.
[94]
H. S. Mason, “Structures and functions of the phenolase complex,” Nature, vol. 177, no. 4498, pp. 79–81, 1956.
[95]
A. M. Mayer, “Polyphenol oxidases in plants and fungi: going places? A review,” Phytochemistry, vol. 67, no. 21, pp. 2318–2331, 2006.
[96]
G. Y. Liu and V. Nizet, “Color me bad: microbial pigments as virulence factors,” Trends in Microbiology, vol. 17, no. 9, pp. 406–413, 2009.
[97]
A. A. Brakhage, K. Langfelder, G. A. Wanner, and J. B. Schmidt, “Pigment biosynthesis and virulence,” in Aspergillus Fumigates Contribution to Microbiology, A. A. Brakhage and J. B. Schmidt, Eds., vol. 2, Karger, Basel, Switzerland, 1999.
[98]
S. E. Baker, “Aspergillus genomics and DHN-melanin conidial pigmentation,” in Aspergillus in the Genomic Era, J. Varga and R. A. Samson, Eds., chapter 2, pp. 73–82, Wageningen Academic Publishers, Wageningen, The Netherlands, 2008.
[99]
A. A. Bell and M. H. Wheeler, “Biosynthesis and functions of fungal melanins,” Annual Review of Phytopathologypp, vol. 24, pp. 411–451, 1986.
[100]
M. J. Butler and A. W. Day, “Fungal melanins: a review,” Canadian Journal of Microbiology, vol. 44, no. 12, pp. 1115–1136, 1998.
[101]
J. M. Henson, M. J. Butler, and A. W. Day, “The dark side of the mycelium: melanins of phytopathogenic fungi,” Annual Review of Phytopathology, vol. 37, pp. 447–471, 1999.
[102]
B. E. Taylor, M. H. Wheeler, and P. J. Szaniszlo, “Evidence for pentaketide melanin biosynthesis in dematiaceous human pathogenic fungi,” Mycologia, vol. 79, no. 2, pp. 320–322, 1987.
[103]
K. Langfelder, M. Streibel, B. Jahn, G. Haase, and A. A. Brakhage, “Biosynthesis of fungal melanins and their importance for human pathogenic fungi,” Fungal Genetics and Biology, vol. 38, no. 2, pp. 143–158, 2003.
[104]
J. D. Nosanchuk and A. Casadevall, “The contribution of melanin to microbial pathogenesis,” Cellular Microbiology, vol. 5, no. 4, pp. 203–223, 2003.
[105]
H. C. Eisenman and A. Casadevall, “Synthesis and assembly of fungal melanin,” Applied Microbiology and Biotechnology, vol. 93, no. 3, pp. 931–940, 2012.
[106]
C. P. Woloshuk, H. D. Sisler, M. C. Tokousbalides, and S. R. Dutky, “Melanin biosynthesis in Pyricularia oryzae: site of tricyclazole inhibition and pathogenicity of melanin-deficient mutants,” Pesticide Biochemistry and Physiology, vol. 14, no. 3, pp. 256–264, 1980.
[107]
A. A. Bell, J. E. Puhalla, W. J. Tolmsoff, and R. D. Stipanovic, “Use of mutants to establish (+)-scytalone as an intermediate in melanin biosynthesis by Verticillium dahliae,” Canadian Journal of Microbiology, vol. 22, no. 6, pp. 787–799, 1976.
[108]
M. H. Wheeler, “Comparisons of fungal melanin biosynthesis in ascomycetous, imperfect and basidiomycetous fungi,” Transactions of the British Mycological Society, vol. 81, no. 1, pp. 29–36, 1983.
[109]
F. de Angelis, A. Arcadi, F. Marinelli et al., “Partial structures of truffle melnins,” Phytochemistry, vol. 43, no. 5, pp. 1103–1106, 1996.
[110]
M. J. Butler, G. Lazarovits, V. J. Higgins, and M.-A. Lachance, “Identification of a black yeast isolated from oak bark as belonging to the genus Phaeococcomyces sp. Analysis of melanin produced by the yeast,” Canadian Journal of Microbiology, vol. 35, no. 7, pp. 728–734, 1989.
[111]
M. H. Wheeler, D. Abramczyk, L. S. Puckhaber et al., “New biosynthetic step in the melanin pathway of Wangiella (Exophiala) dermatitidis: evidence for 2-acetyl-1,3,6,8-tetrahydroxynaphthalene as a novel precursor,” Eukaryotic Cell, vol. 7, no. 10, pp. 1699–1711, 2008.
[112]
B. S. Moore, “Discovery of a new bacterial polyketide biosynthetic pathway,” ChemBioChem, vol. 2, no. 1, pp. 35–38, 2001.
[113]
E. Bourquelot and G. Bertrand, “Le bleuissement et le noircissement des champignons,” Comptes Rendus Biologies, vol. 47, pp. 582–584, 1895.
[114]
K. Boekelheide, D. G. Graham, P. D. Mize, and E. Koo h., “Melanocytotoxicity and the mechanism of activation of γ-L-glutaminyl-4-hydroxybenzene,” Journal of Investigative Dermatology, vol. 75, no. 4, pp. 322–327, 1980.
[115]
H. Stüssi and D. M. Rast, “The biosynthesis and possible function of γ-glutaminyl-4-hydroxybenzene in Agaricus bisporus,” Phytochemistry, vol. 20, no. 10, pp. 2347–2352, 1981.
[116]
A. E. Ross, D. L. Nagel, and B. Toth, “Ocurrence, stability and decomposition of β-N[γ-L(+)-glutamyl]-4-hydroxymethylphenylhydrazine (agaritine) from the mushroom Agaricus bisporus,” Food and Chemical Toxicology, vol. 20, no. 6, pp. 903–907, 1982.
[117]
W.-N. Gao, D.-Q. Wei, Y. Li et al., “Agaritine and its derivatives are potential inhibitors against HIV proteases,” Medicinal Chemistry, vol. 3, no. 3, pp. 221–226, 2007.
[118]
J. C. Espín, S. Jolivet, A. Overeem, and H. J. Wichers, “Agaritine from Agaricus bisporus is capable of preventing melanin formation,” Phytochemistry, vol. 50, no. 4, pp. 555–563, 1999.
[119]
A. Casadevall, A. L. Rosas, and J. D. Nosanchuk, “Melanin and virulence in Cryptococcus neoformans,” Current Opinion in Microbiology, vol. 3, no. 4, pp. 354–358, 2000.
[120]
I. Polacheck, V. J. Hearing, and K. J. Kwon-Chung, “Biochemical studies of phenoloxidase and utilization of catecholamines in Cryptococcus neoformans,” Journal of Bacteriology, vol. 150, no. 3, pp. 1212–1220, 1982.
[121]
I. Polacheck and K. J. Kwon-Chung, “Melanogenesis in Cryptococcus neoformans,” Journal of General Microbiology, vol. 134, no. 4, pp. 1037–1041, 1988.
[122]
H. C. Eisenman, M. Mues, S. E. Weber et al., “Cryptococcus neoformans laccase catalyses melanin synthesis from both D- and L-DOPA,” Microbiology, vol. 153, no. 12, pp. 3954–3962, 2007.
[123]
S. Frases, A. Salazar, E. Dadachova, and A. Casadevall, “Cryptococcus neoformans can utilize the bacterial melanin precursor homogentisic acid for fungal melanogenesis,” Applied and Environmental Microbiology, vol. 75, no. 2, pp. 493–503, 2009.
[124]
J. Schmaler-Ripcke, V. Sugareva, P. Gebhardt et al., “Production of pyomelanin, a second type of melanin, via the tyrosine degradation pathway in Aspergillus fumigatus,” Applied and Environmental Microbiology, vol. 75, no. 2, pp. 493–503, 2009.
[125]
R. C. R. Gon?alves, H. C. F. Lisboa, and S. R. Pombeiro-Sponchiado, “Characterization of melanin pigment produced by Aspergillus nidulans,” World Journal of Microbiology and Biotechnology, vol. 28, no. 4, pp. 1467–1474, 2012.
[126]
Y. Satyawali and M. Balakrishnan, “Wastewater treatment in molasses-based alcohol distilleries for COD and color removal: a review,” Journal of Environmental Management, vol. 86, no. 3, pp. 481–497, 2008.
[127]
J. R. Mencher and A. H. Heim, “Melanin biosynthesis by Streptomyces lavendulae,” Microbiology, vol. 28, no. 4, pp. 665–670, 1962.
[128]
T. Arai and Y. Mikami, “Chromogenicity of streptomyces,” Applied Microbiology, vol. 23, no. 2, pp. 402–406, 1972.
[129]
K. Lerch and L. Ettinger, “Purification and characterization of a tyrosinase from Streptomyces glaucescens,” European Journal of Biochemistry, vol. 31, no. 3, pp. 427–437, 1972.
[130]
M. P. Jackman, A. Hajnal, and K. Lerch, “Albino mutants of Streptomyces glaucescens tyrosinase,” Biochemical Journal, vol. 274, no. 3, pp. 707–713, 1991.
[131]
D. López-serrano, A. Sanchez-Amat, and F. Solano, “Cloning and molecular characterization of a SDS-activated tyrosinase from Marinomonas mediterranea,” Pigment Cell Research, vol. 15, no. 2, pp. 104–111, 2002.
[132]
D. López-Serrano, F. Solano, and A. Sanchez-Amat, “Identification of an operon involved in tyrosinase activity and melanin synthesis in Marinomonas mediterranea,” Gene, vol. 342, no. 1, pp. 179–187, 2004.
[133]
A. E. Aghajanyan, A. A. Hambardzumyan, A. S. Hovsepyan, R. A. Asaturian, A. A. Vardanyan, and A. A. Saghiyan, “Isolation, purification and physicochemical characterization of water-soluble Bacillus thuringiensis melanin,” Pigment Cell Research, vol. 18, no. 2, pp. 130–135, 2005.
[134]
Y. Chen, Y. Deng, J. Wang, J. Cai, and G. Ren, “Characterization of melanin produced by a wild-type strain of Bacillus thuringiensis,” Journal of General and Applied Microbiology, vol. 50, no. 4, pp. 183–188, 2004.
[135]
K. R. Patel, J. A. Wyman, K. A. Patel, and B. J. Burden, “A mutant of Bacillus thuringiensis producing a dark-brown pigment with increased UV resistance and insecticidal activity,” Journal of Invertebrate Pathology, vol. 67, no. 2, pp. 120–124, 1996.
[136]
T. A. Barnett, D. Valenzuela, S. Riner, and J. H. Hageman, “Production by Bacillis subtilis of brown sporulation-association pigments,” Canadian Journal of Microbiology, vol. 29, no. 1, pp. 96–101, 1983.
[137]
M. T. Cubo, A. M. Buendia-Claveria, J. E. Beringer, and J. E. Ruiz-Sainz, “Melanin production by Rhizobium strains,” Applied and Environmental Microbiology, vol. 54, no. 7, pp. 1812–1817, 1988.
[138]
S. Shivprasad and W. J. Page, “Catechol formation and melanization by Na+-dependent Azotobacter chroococcum: a protective mechanism for aeroadaptation?” Applied and Environmental Microbiology, vol. 55, no. 7, pp. 1811–1817, 1989.
[139]
H. L. C. Meuzelaar, K. Haider, B. R. Nagar, and J. P. Martin, “Comparative studies of pyrolysis-mass spectra of melanins, model phenolic polymers, and humic acids,” Geoderma, vol. 17, no. 3, pp. 239–252, 1977.
[140]
S. Paim, L. F. Linhares, A. S. Mangrich, and J. P. Martin, “Characterization of fungal melanins and soil humic acids by chemical analysis and infrared spectroscopy,” Biology and Fertility of Soils, vol. 10, no. 1, pp. 72–76, 1990.
[141]
J. Trias, M. Vinas, J. Guinea, and J. G. Loren, “Brown pigmentation in Serratia marcescens cultures associated with tyrosine metabolism,” Canadian Journal of Microbiology, vol. 35, no. 11, pp. 1037–1042, 1989.
[142]
E. Yabuuchi and A. Ohyama, “Characterization of pyomelanin producing strains of Pseudomonas aeruginosa,” International Journal of Systematic Bacteriology, vol. 22, pp. 53–64, 1972.
[143]
J. Ogunnariwo and J. M. T. Hamilton Miller, “Brown and red pigmented Pseudomonas aeruginosa: differentiation between melanin and pyorubrin,” Journal of Medical Microbiology, vol. 8, no. 1, pp. 199–203, 1975.
[144]
U. Ruetschi, B. Odelhog, S. Lindstedt, J. Barros-Soderling, B. Persson, and H. Jornvall, “Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme,” European Journal of Biochemistry, vol. 205, no. 2, pp. 459–466, 1992.
[145]
C. Ruzafa, F. Solano, and A. Sanchez-Amat, “The protein encoded by the Shewanella colwelliana melA gene is a p-hydroxyphenylpyruvate dioxygenase,” FEMS Microbiology Letters, vol. 124, no. 2, pp. 179–184, 1994.
[146]
V. E. Coyne and L. Al-Harthi, “Induction of melanin biosynthesis in Vibrio cholerae,” Applied and Environmental Microbiology, vol. 58, no. 9, pp. 2861–2865, 1992.
[147]
C. Ruzafa, A. Sanchez-Amat, and F. Solano, “Characterization of the melanogenic system in Vibrio cholerae, ATCC 14035,” Pigment Cell Research, vol. 8, no. 3, pp. 147–152, 1995.
[148]
A. Sanchez-Amat, C. Ruzafa, and F. Solano, “Comparative tyrosine degradation in Vibrio cholerae strains. The strain ATCC 14035 as a prokaryotic melanogenic model of homogentisate-releasing cell,” Comparative Biochemistry and Physiology B, vol. 119, no. 3, pp. 557–562, 1998.
[149]
K. E. Keith, L. Killip, P. He, G. R. Moran, and M. A. Valvano, “Burkholderia cenocepacia C5424 produces a pigment with antioxidant properties using a homogentisate intermediate,” Journal of Bacteriology, vol. 189, no. 24, pp. 9057–9065, 2007.
[150]
H. Lee, S. M. Dellatore, W. M. Miller, and P. B. Messersmith, “Mussel-inspired surface chemistry for multifunctional coatings,” Science, vol. 318, no. 5849, pp. 426–430, 2007.
[151]
A. A. R. Watt, J. P. Bothma, and P. Meredith, “The supramolecular structure of melanin,” Soft Matter, vol. 5, no. 19, pp. 3754–3760, 2009.
[152]
N. Kollias, “The spectroscopy of human melanin pigmentation,” in Melanin: Its Role in Human Photoprotection, pp. 31–38, Valdenmar Publishing, 1995.
[153]
G. Goodman and D. Bercovich, “Melanin directly converts light for vertebrate metabolic use: heuristic thoughts on birds, Icarus and dark human skin,” Medical Hypotheses, vol. 71, no. 2, pp. 190–202, 2008.
[154]
B. R. O. de Montellano, “Melanin, afrocentricity, and pseudoscience,” American Journal of Physical Anthropology, vol. 92, no. 17, pp. 33–58, 1993.
[155]
B. L. Diffey, E. Healy, A. J. Thody, and J. L. Rees, “Melanin, melanocytes, and melanoma,” The Lancet, vol. 346, no. 8991-8992, p. 1713, 1995.
[156]
R. B. Setlow, E. Grist, K. Thompson, and A. D. Woodhead, “Wavelengths effective in induction of malignant melanoma,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 14, pp. 6666–6670, 1993.
[157]
E. Kvam and R. M. Tyrrell, “The role of melanin in the induction of oxidative DNA base damage by ultraviolet A irradiation of DNA or melanoma cells,” Journal of Investigative Dermatology, vol. 113, no. 2, pp. 209–213, 1999.
[158]
F. P. Noonan, M. R. Zaidi, A. Wolnicka-Glubisz, et al., “Melanoma induction by ultraviolet A but not ultraviolet B radiation requires melanin pigment,” Nature Communications, vol. 3, article 884, 2012.
[159]
E. C. de Fabo, F. P. Noonan, T. Fears, and G. Merlino, “Ultraviolet B but not ultraviolet A radiation initiates melanoma,” Cancer Research, vol. 64, no. 18, pp. 6372–6376, 2004.
[160]
M. R. Chedekel, “Photochemistry and photobiology of epidermal melanins,” Photochemistry and Photobiology, vol. 35, no. 6, pp. 881–885, 1982.
[161]
E. Wenczl, G. P. van der Schans, L. Roza et al., “(Pheo)melanin photosensitizes UVA-induced DNA damage in cultured human melanocytes,” Journal of Investigative Dermatology, vol. 111, no. 4, pp. 678–682, 1998.
[162]
R. C. Sealy, J. S. Hyde, C. C. Felix, et al., “Novel free radicals in synthetic and natural pheomelanins: distinction between dopa melanins and cysteinyldopa melanins by ESR spectroscopy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no. 9 I, pp. 2885–2889, 1982.
[163]
H. Z. Hill and G. J. Hill, “UVA, pheomelanin and the carcinogenesis of melanoma,” Pigment Cell Research, vol. 13, no. 8, pp. 140–144, 2000.
[164]
D. Mitra, X. Luo, A. Morgan, et al., “An ultraviolet-radiation-independent pathway to melanoma carcinogenesis in the red hair/fair skin,” Nature, vol. 491, pp. 449–453, 2012.
[165]
T. B. Fitzpatrick, “Albinism: some thoughts on the color problem and integration of dermatology and medicine,” The Journal of Investigative Dermatology, vol. 35, pp. 209–214, 1960.
[166]
S. J. Charles, J. S. Green, J. W. Grant, J. R. W. Yates, and A. T. Moore, “Clinical features of affected males with X linked ocular albinism,” British Journal of Ophthalmology, vol. 77, no. 4, pp. 222–227, 1993.
[167]
W. S. Oetting, “The tyrosinase gene and oculocutaneous albinism type 1 (OCA1): a model for understanding the molecular biology of melanin formation,” Pigment Cell Research, vol. 13, no. 5, pp. 320–325, 2000.
[168]
W. S. Oetting, J. P. Fryer, S. Shriram, and R. A. King, “Oculocutaneous albinism type 1: the last 100 years,” Pigment Cell Research, vol. 16, no. 3, pp. 307–311, 2003.
[169]
L. Montoliu, K. Gronskov, A. H. Wei, et al., “Increasing the complexity: new genes and new types of albinism,” Pigment Cell Melanoma Research, vol. 27, no. 1, pp. 11–18, 2014.
[170]
C. G. Summers, “Albinism: classification, clinical characteristics, and recent findings,” Optometry and Vision Science, vol. 86, no. 6, pp. 659–662, 2009.
[171]
D. Durham-Pierre, J. M. Gardner, Y. Nakatsu et al., “African origin of an intragenic deletion of the human P gene in tyrosinase positive oculocutaneous albinism,” Nature Genetics, vol. 7, no. 2, pp. 176–179, 1994.
[172]
S.-T. Lee, R. D. Nicholls, R. E. Schnur et al., “Diverse mutations of the P gene among African—Americans with type II (tyrosinase-positive) oculocutaneous albinism (OCA2),” Human Molecular Genetics, vol. 3, no. 11, pp. 2047–2051, 1994.
[173]
F. Hermansky and P. Pudlak, “Albinism associated with hemorrhagic diathesis and unusual pigmented reticular cells in the bone marrow: report of two cases with histochemical studies,” Blood, vol. 14, no. 2, pp. 162–169, 1959.
[174]
W. Introne, R. E. Boissy, and W. A. Gahl, “Clinical, molecular, and cell biological aspects of Chediak-Higashi syndrome,” Molecular Genetics and Metabolism, vol. 68, no. 2, pp. 283–303, 1999.
[175]
H. Z. Hill, “The function of melanin or six blind people examine an elephant,” BioEssays, vol. 14, no. 1, pp. 49–56, 1992.
[176]
Z. Wang, J. Dillon, and E. R. Gaillard, “Antioxidant properties of melanin in retinal pigment epithelial cells,” Photochemistry and Photobiology, vol. 82, no. 2, pp. 474–479, 2006.
[177]
R. Sarangarajan and S. P. Apte, “Melanization and phagocytosis: implications for age related macular degeneration,” Molecular Vision, vol. 11, pp. 482–490, 2005.
[178]
M. S. Hosseini, B. N. Araabi, and H. Soltanian-Zadeh, “Pigment melanin: pattern for iris recognition,” IEEE Transactions on Instrumentation and Measurement, vol. 59, no. 4, pp. 792–804, 2010.
[179]
A. M. Meyer zum Gottesberge, “Physiology and pathophysiology of inner ear melanin,” Pigment Cell Research, vol. 1, no. 4, pp. 238–249, 1988.
[180]
A. P. Read, “Waardenburg syndrome,” Advances in Oto-Rhino-Laryngology, vol. 56, pp. 32–38, 2000.
[181]
F. A. Zucca, E. Basso, F. A. Cupaioli, et al., “Neuromelanin of the human substantia nigra: an update,” Neurotoxicity Research, vol. 25, no. 1, pp. 13–23, 2013.
[182]
K. L. Double, M. Gerlach, V. Schünemann et al., “Iron-binding characteristics of neuromelanin of the human substantia nigra,” Biochemical Pharmacology, vol. 66, no. 3, pp. 489–494, 2003.
[183]
L. Zecca, A. Stroppolo, A. Gatti et al., “The role of iron and molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 26, pp. 9843–9848, 2004.
[184]
L. Zecca, F. A. Zucca, A. Albertini, E. Rizzio, and R. G. Fariello, “A proposed dual role of neuromelanin in the pathogenesis of Parkinson's disease,” Neurology, vol. 67, no. 7, supplement 2, pp. S8–S11, 2006.
[185]
C. R. Borges, J. C. Roberts, D. G. Wilkins, and D. E. Rollins, “Cocaine, benzoylecgonine, amphetamine, and N-acetylamphetamine binding to melanin subtypes,” Journal of Analytical Toxicology, vol. 27, no. 3, pp. 125–134, 2003.
[186]
O. Karlsson and N. G. Lindquist, “Melanin affinity and its possible role in neurodegeneration,” Journal of Neural Transmission, vol. 120, no. 12, pp. 1623–1630, 2013.
[187]
R. H. C. Bonser, “Melanin and the abrasion resistance of feathers,” Condor, vol. 97, pp. 590–591, 1995.
[188]
I. Galván and C. Alonso-Alvarez, “An intracellular antioxidant determines the expression of a melanin-based signal in a bird,” PLoS ONE, vol. 3, no. 10, Article ID e3335, 2008.
[189]
K. J. McGraw, “An update on the honesty of melanin-based color signals in birds,” Pigment Cell and Melanoma Research, vol. 21, no. 2, pp. 133–138, 2008.
[190]
J. Zi, X. Yu, Y. Li et al., “Coloration strategies in peacock feathers,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 22, pp. 12576–12578, 2003.
[191]
S. C. Griffith, T. H. Parker, and V. A. Olson, “Melanin- versus carotenoid-based sexual signals: is the difference really so black and red?” Animal Behaviour, vol. 71, no. 4, pp. 749–763, 2006.
[192]
D. Stuart-Fox and A. Moussalli, “Camouflage, communication and thermoregulation: lessons from colour changing organisms,” Philosophical Transactions of the Royal Society B, vol. 364, no. 1516, pp. 463–470, 2009.
[193]
A. M. Bauer, “Peritoneal pigmentation and generic allocation in the Chamaeleonidae,” African Journal of Herpetology, vol. 46, no. 2, pp. 117–123, 1997.
[194]
G. Sichel, M. Scalia, F. Mondio, and C. Corsaro, “The amphibian kupffer cells build and demolish melanosomes: an ultrastructural point of view,” Pigment Cell Research, vol. 10, no. 5, pp. 271–287, 1997.
[195]
A. J. Nappi and E. Vass, “Melanogenesis and the generation of cytotoxic molecules during insect cellular immune reactions,” Pigment Cell Research, vol. 6, no. 3, pp. 117–126, 1993.
[196]
I. González-Santoyo and A. Córdoba-Aguilar, “Phenoloxidase: a key component of the insect immune system,” Entomologia Experimentalis et Applicata, vol. 142, no. 1, pp. 1–16, 2012.
[197]
J. R. Whitaker and C. Y. Lee, “Enzymatic browning and its prevention. Recent advances in chemistry of enzymatic browning,” Trends in Food Science & Technology, vol. 6, no. 6, pp. 195–200, 1995.
[198]
R. Yoruk and M. R. Marshall, “Physicochemical properties and function of plant polyphenol oxidase: a review,” Journal of Food Biochemistry, vol. 27, no. 5, pp. 361–422, 2003.
[199]
E. Dadachova and A. Casadevall, “Ionizing radiation: how fungi cope, adapt, and exploit with the help of melanin,” Current Opinion in Microbiology, vol. 11, no. 6, pp. 525–531, 2008.
[200]
I. Galván, T. A. Mousseau, and A. P. M?ller, “Bird population declines due to radiation exposure at Chernobyl are stronger in species with pheomelanin-based coloration,” Oecologia, vol. 165, no. 4, pp. 827–835, 2011.
[201]
M.-J. Kuo and M. Alexander, “Inhibition of the lysis of fungi by melanins,” Journal of Bacteriology, vol. 94, no. 3, pp. 624–629, 1967.
[202]
V. D. Kuznetsov, S. N. Filippova, and A. M. Rybakova, “Nature of the brown pigment and the composition of phenol oxidases in Streptomyces galbus,” Mikrobiologiya, vol. 53, no. 2, pp. 251–256, 1984.
[203]
M.-F. Hullo, I. Moszer, A. Danchin, and I. Martin-Verstraete, “CotA of Bacillus subtilis is a copper-dependent laccase,” Journal of Bacteriology, vol. 183, no. 18, pp. 5426–5430, 2001.
[204]
R. J. Howard and M. A. Ferrari, “Role of melanin in appressorium function,” Experimental Mycology, vol. 13, no. 4, pp. 403–418, 1989.
[205]
M. Abbas, F. D'Amico, L. Morresi et al., “Structural, electrical, electronic and optical properties of melanin films,” European Physical Journal E, vol. 28, no. 3, pp. 285–291, 2009.
[206]
J. P. Bothma, J. de Boor, U. Divakar, P. E. Schwenn, and P. Meredith, “Device-quality electrically conducting melanin thin films,” Advanced Materials, vol. 20, no. 18, pp. 3539–3542, 2008.
[207]
M. Apte, G. Girme, A. Bankar, A. RaviKumar, and S. Zinjarde, “3,4-dihydroxy-L-phenylalanine-derived melanin from Yarrowia lipolytica mediates the synthesis of silver and gold nanostructures,” Journal of Nanobiotechnology, vol. 11, article 2, 2013.
[208]
H. S. Raper, “The aerobic oxidases,” Physiol, vol. 8, pp. 245–282, 1928.
[209]
A. B. Lerner and T. B. Fitzpatrick, “Biochemistry of melanin formation,” Physiological Reviews, vol. 30, no. 1, pp. 91–126, 1950.
[210]
A. Sanchez-Ferrer, J. N. Rodriguez-Lopez, F. Garcia-Canovas, and F. Garcia-Carmona, “Tyrosinase: a comprehensive review of its mechanism,” Biochimica et Biophysica Acta, vol. 1247, no. 1, pp. 1–11, 1995.
[211]
C. J. Cooksey, P. J. Garratt, E. J. Land et al., “Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase,” Journal of Biological Chemistry, vol. 272, no. 42, pp. 26226–26235, 1997.
[212]
C. Olivares and F. Solano, “New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins,” Pigment Cell and Melanoma Research, vol. 22, no. 6, pp. 750–760, 2009.
[213]
G. Agrup, B. Falck, and B. M. Kennedy, “Formation of cysteinyldopa from glutathionedopa in melanoma,” Acta Dermato-Venereologica, vol. 55, no. 1, pp. 1–3, 1975.
[214]
P. Aroca, J. C. Garcia-Borron, F. Solano, and J. A. Lozano, “Regulation of mammalian melanogenesis I: partial purification and characterization of a dopachrome converting factor: dopachrome tautomerase,” Biochimica et Biophysica Acta, vol. 1035, no. 3, pp. 266–275, 1990.
[215]
F. Solano, “Biochemistry of mammalian pigmentation. Enzymatic regulation of the melanogenesis,” in Cell and Tissue Culture Models in Dermatological Research, A. Bernd, J. Bereiter-Hahn, F. Hevert, and H. Holzmann, Eds., pp. 135–147, Springer, Berlin, Germany, 1993.
[216]
F. Solano, C. Jiménez-Cervantes, J. H. Martínez-Liarte, J. C. García-Borrón, J. R. Jara, and J. A. Lozano, “Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase,” Biochemical Journal, vol. 313, no. 2, pp. 447–453, 1996.
[217]
J. R. Jara, F. Solano, and J. A. Lozano, “Assays for mammalian tyrosinase: a comparative study,” Pigment Cell Research, vol. 1, no. 5, pp. 332–339, 1988.
[218]
C. Jimenez-Cervantes, F. Solano, T. Kobayashi et al., “A new enzymatic function in the melanogenic pathway. The 5,6- dihydroxyindole-2-carboxylic acid oxidase activity of tyrosinase-related protein-1 (TRP1),” Journal of Biological Chemistry, vol. 269, no. 27, pp. 17993–18000, 1994.
[219]
R. E. Boissy, C. Sakai, H. Zhao, T. Kobayashi, and V. J. Hearing, “Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1,” Experimental Dermatology, vol. 7, no. 4, pp. 198–204, 1998.
[220]
C. Olivares, C. Jiménez-Cervantes, J. A. Lozano, F. Solano, and J. C. García-Borrón, “The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase,” Biochemical Journal, vol. 354, no. 1, pp. 131–139, 2001.
[221]
A. Palumbo, M. D'Ischia, G. Misuraca, L. De Martino, and G. Prota, “A new dopachrome-rearranging enzyme from the ejected ink of the cuttlefish Sepia officinalis,” Biochemical Journal, vol. 299, no. 3, pp. 839–844, 1994.
[222]
S. Chintala, W. Li, M. L. Lamoreux et al., “Slc7a11 gene controls production of pheomelanin pigment and proliferation of cultured cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 31, pp. 10964–10969, 2005.
[223]
J. R. Jara, P. Aroca, F. Solano, J. H. Martinez, and J. A. Lozano, “The role of sulfhydryl compounds in mammalian melanogenesis: the effect of cysteine and glutathione upon tyrosinase and the intermediates of the pathway,” Biochimica et Biophysica Acta, vol. 967, no. 2, pp. 296–303, 1988.
[224]
S. Naish-Byfield, C. J. Cooksey, and P. A. Riley, “Oxidation of monohydric phenol substrates by tyrosinase: effect of dithiothreitol on kinetics,” Biochemical Journal, vol. 304, no. 1, pp. 155–162, 1994.
[225]
E. Benedito, C. Jimenez-Cervantes, J. D. Cubillana, F. Solano, J. A. Lozano, and J. C. Garcia-Borron, “Biochemical characterization of the melanogenic system in the eye of adult rodents,” Biochimica et Biophysica Acta, vol. 1252, no. 2, pp. 217–224, 1995.
[226]
A. Biesemeier, F. Kreppel, S. Kochanek, and U. Schraermeyer, “The classical pathway of melanogenesis is not essential for melanin synthesis in the adult retinal pigment epithelium,” Cell and Tissue Research, vol. 339, no. 3, pp. 551–560, 2010.
[227]
E. Benedito, C. Jiménez-Cervantes, D. Pérez et al., “Melanin formation in the inner ear is catalyzed by a new tyrosine hydroxylase kinetically and structurally different from tyrosinase,” Biochimica et Biophysica Acta, vol. 1336, no. 1, pp. 59–72, 1997.
[228]
K. Ikemoto, I. Nagatsu, S. Ito, R. A. King, A. Nishimura, and T. Nagatsu, “Does tyrosinase exist in neuromelanin-pigmented neurons in the human substantia nigra?” Neuroscience Letters, vol. 253, no. 3, pp. 198–200, 1998.
[229]
J. Matsunaga, D. Sinha, L. Pannell et al., “Enzyme activity of macrophage migration inhibitory factor toward oxidized catecholamines,” Journal of Biological Chemistry, vol. 274, no. 6, pp. 3268–3271, 1999.
[230]
R. R. Mills, C. R. Lake, and W. L. Alworth, “Biosynthesis of N-acetyl dopamine by the American cockroach,” Journal of Insect Physiology, vol. 13, no. 10, pp. 1539–1546, 1967.
[231]
S. J. Saul and M. Sugumaran, “o-Quinone/quinone methide isomerase: a novel enzyme preventing the destruction of self-matter by phenoloxidase-generated quinones during immune response in insects,” FEBS Letters, vol. 249, no. 2, pp. 155–158, 1989.
[232]
M. Sugumaran, L. B. Giglio, H. Kundzicz, S. Saul, and V. Semensi, “Studies on the enzymes involved in puparial cuticle sclerotization in Drosophila melanogaster,” Archives of Insect Biochemistry and Physiology, vol. 19, no. 4, pp. 271–283, 1992.
[233]
M. Sugumaran, H. Dali, V. Semensi, and B. Hennigan, “Tyrosinase-catalyzed unusual oxidative dimerization of 1,2-dehydro-N-acetyldopamine,” The Journal of Biological Chemistry, vol. 262, no. 22, pp. 10546–10549, 1987.
[234]
H. S. Mason, “The chemistry of melanin; mechanism of the oxidation of catechol by,” The Journal of Biological Chemistry, vol. 181, no. 2, pp. 803–812, 1949.
[235]
N. A. Bisko, V. V. Shcherba, and N. Y. Mitropolskaya, “Study of melanin complex from medicinal mushroom Phellinus robustus (P. Karst.) Bourd. et Galz. (Aphyllophoromycetideae),” International Journal of Medicinal Mushrooms, vol. 9, no. 2, pp. 177–184, 2007.
[236]
S. Jolivet, N. Arpin, H. J. Wichers, and G. Pellon, “Agaricus bisporus browning: a review,” Mycological Research, vol. 102, no. 12, pp. 1459–1483, 1998.
[237]
H. S. Mason, W. L. Fowlks, and E. Peterson, “Oxygen transfer and electron transport by the phenolase complex,” Journal of the American Chemical Society, vol. 107, pp. 4015–4027, 1955.
[238]
J. C. García-Borrón and F. Solano, “Molecular anatomy of tyrosinase and its related proteins: beyond the histidine-bound metal catalytic center,” Pigment Cell Research, vol. 15, no. 3, pp. 162–173, 2002.
[239]
C. Gessard, “Sur la formation du pigment méanique dans les tumeurs du cheval,” Comptes Rendus de l'Académie des Sciences, vol. 136, pp. 1086–1088, 1903.
[240]
B. Bloch, “Das Pigment,” in Handbuch der Haut und Geschlechtskrankeiten, J. Jadassohn, Ed., vol. 1, part 1, pp. 343–451, Springer, Berlin, Germany, 1927.
[241]
G. H. Hogeboom and M. H. Adams, “Mammalian tyrosinase and dopa oxidase,” The Journal of Biological Chemistry, vol. 145, pp. 273–279, 1942.
[242]
A. B. Lerner, T. B. Fitzpatrick, E. Calkins, and W. H. Summerson, “Mammalian tyrosinase: preparation and properties,” The Journal of Biological Chemistry, vol. 178, pp. 185–195, 1949.
[243]
A. M. Korner and J. Pawelek, “Dopachrome conversion: a possible control point in melanin biosynthesis,” Journal of Investigative Dermatology, vol. 75, no. 2, pp. 192–195, 1980.
[244]
F. Solano, J. H. Martinez-Liarte, C. Jimenenz-Cervantes, J. C. Garcia-Borron, and J. A. Lozano, “Dopachrome tautomerase is a zinc-containing enzyme,” Biochemical and Biophysical Research Communications, vol. 204, no. 3, pp. 1243–1250, 1994.
[245]
M. Furumura, F. Solano, N. Matsunaga, C. Sakai, R. A. Spritz, and V. J. Hearing, “Metal ligand-binding specificities of the tyrosinase-related proteins,” Biochemical and Biophysical Research Communications, vol. 242, no. 3, pp. 579–585, 1998.
[246]
A. M. Mayer and R. C. Staples, “Laccase: new functions for an old enzyme,” Phytochemistry, vol. 60, no. 6, pp. 551–565, 2002.
[247]
E. Fernández, A. Sanchez-Amat, and F. Solano, “Location and catalytic characteristics of a multipotent bacterial polyphenol oxidase,” Pigment Cell Research, vol. 12, no. 5, pp. 331–339, 1999.
[248]
F. H. Claus and H. Decker, “Bacterial tyrosinases,” Systematic and Applied Microbiology, vol. 29, no. 1, pp. 3–14, 2006.
[249]
M. Fairhead and L. Th?ny-Meyer, “Bacterial tyrosinases: old enzymes with new relevance to biotechnology,” New Biotechnology, vol. 29, no. 2, pp. 183–191, 2012.
[250]
A. Sanchez-Amat, P. Lucas-Elío, E. Fernández, J. C. García-Borrón, and F. Solano, “Molecular cloning and functional characterization of a unique multipotent polyphenol oxidase from Marinomonas mediterranea,” Biochimica et Biophysica Acta, vol. 1547, no. 1, pp. 104–116, 2001.
[251]
D. Hernández-Romero, A. Sanchez-Amat, and F. Solano, “A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio: role of the seventh histidine and accessibility to the active site,” FEBS Journal, vol. 273, no. 2, pp. 257–270, 2006.
[252]
Y.-J. Kim and H. Uyama, “Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future,” Cellular and Molecular Life Sciences, vol. 62, no. 15, pp. 1707–1723, 2005.
[253]
F. Solano, S. Briganti, M. Picardo, and G. Ghanem, “Hypopigmenting agents: an updated review on biological, chemical and clinical aspects,” Pigment Cell Research, vol. 19, no. 6, pp. 550–571, 2006.
[254]
L. Vámos-Vigyázó, “Prevention of enzymatic browning in fruits and vegetables. A review of principles and practice,” in Enzymatic Browning and Its Prevention, vol. 600 of ACS Symposium Series, chapter 4, pp. 49–62, 1995.
[255]
O. Nerya, R. Ben-Arie, T. Luzzatto, R. Musa, S. Khativ, and J. Vaya, “Prevention of Agaricus bisporus postharvest browning with tyrosinase inhibitors,” Postharvest Biology and Technology, vol. 39, no. 3, pp. 272–277, 2006.
[256]
M. R. Loizzo, R. Tundis, and F. Menichini, “Natural and synthetic tyrosinase inhibitors as antibrowning agents: an update,” Comprehensive Reviews in Food Science and Food Safety, vol. 11, no. 4, pp. 378–398, 2012.
[257]
C. E. Turick, L. S. Tisa, and F. Caccavo Jr., “Melanin production and use as a soluble electron shuttle for Fe(III) oxide reduction and as a terminal electron acceptor by Shewanella algae BrY,” Applied and Environmental Microbiology, vol. 68, no. 5, pp. 2436–2444, 2002.
[258]
G. Szabo, “Photobiology of melanogenesis: cytological aspects with special reference to differences in racial coloration,” in The Pigmentary SystemAdvances in Biology of the Skin, W. Montagna and F. Hu, Eds., vol. 8, pp. 379–396, Pergamon Press, New York, NY, USA, 1967.
[259]
Y. Yamaguchi, M. Brenner, and V. J. Hearing, “The regulation of skin pigmentation,” Journal of Biological Chemistry, vol. 282, no. 38, pp. 27557–27561, 2007.
[260]
A. Chakraborty, A. Slominski, G. Ermak, J. Hwang, and J. Pawelek, “Ultraviolet B and melanocyte-stimulating hormone (MSH) stimulate mRNA production for αMSH receptors and proopiomelanocortin-derived peptides in mouse melanoma cells and transformed keratinocytes,” Journal of Investigative Dermatology, vol. 105, no. 5, pp. 655–659, 1995.
[261]
T. B. Fitzpatrick and A. S. Breathnach, “Das epidermale melanin-einheit-system,” Dermatologische Wochenschrift, vol. 747, pp. 481–489, 1963.
[262]
G. Szabó, A. B. Gerald, M. A. Pathak, and T. B. Fitzpatrick, “Racial differences in the fate of melanosomes in human epidermis,” Nature, vol. 222, no. 5198, pp. 1081–1082, 1969.
[263]
T. Caro, “The adaptive significance of coloration in mammals,” BioScience, vol. 55, no. 2, pp. 125–136, 2005.
[264]
S. K. Singh, C. Nizard, R. Kurfurst, F. Bonte, S. Schnebert, and D. J. Tobin, “The silver locus product (Silv/gp100/Pmel17) as a new tool for the analysis of melanosome transfer in human melanocyte-keratinocyte co-culture,” Experimental Dermatology, vol. 17, no. 5, pp. 418–426, 2008.
[265]
A. K. Tarafder, G. Bolasco, M. S. Correia, et al., “Rab11b mediates melanin transfer between donor melanocytes and acceptor keratinocytes via coupled exo/endocytosis,” Journal Investigative Dermatology, 2013.
[266]
D. C. Barral and M. C. Seabra, “The melanosome as a model to study organelle motility in mammals,” Pigment Cell Research, vol. 17, no. 2, pp. 111–118, 2004.
[267]
R. A. Sturm, R. D. Teasdale, and N. F. Box, “Human pigmentation genes: identification, structure and consequences of polymorphic variation,” Gene, vol. 277, no. 1-2, pp. 49–62, 2001.
[268]
A. Samokhvalov, L. Hong, Y. Liu et al., “Oxidation potentials of human eumelanosomes and pheomelanosomes,” Photochemistry and Photobiology, vol. 81, no. 1, pp. 145–148, 2005.
[269]
M. Goedert, “Alpha-synuclein and neurodegenerative diseases,” Nature Reviews Neuroscience, vol. 2, no. 7, pp. 492–501, 2001.
[270]
T. Pan, J. Zhu, W.-J. Hwu, and J. Jankovic, “The role of alpha-synuclein in melanin synthesis in melanoma and dopaminergic neuronal cells,” PLoS ONE, vol. 7, no. 9, Article ID e45183, 2012.