全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Remote Control of Bovine Catalase Activity with Specific Frequencies of Human and Bovine Catalase with and without Bound NADP+

DOI: 10.4236/aer.2024.122002, PP. 17-34

Keywords: Remote Control, Catalase, Frequency, Rate Promoting Vibration (RPV), NADP

Full-Text   Cite this paper   Add to My Lib

Abstract:

Remote control enzyme technology is widely used today through resonance. In this study, we showed that the use of frequencies of the catalase enzyme itself to increase enzymatic rate is successful not only in test tubes but also remotely. The present study also suggests that, under optimal temperature, the use of bovine catalase frequency (the specific frequency of that enzyme) has a superior rate promoting vibration than the human catalase frequency, and so increases very significantly the chemical rate of bovine catalase (about 120% at 40?C). It also suggests that bovine catalase subjected to bovine and human frequencies with catalase bound NADP+ experienced more resonance weight towards NADP+ and so were more slowly reduced back to catalase bound NADPH, increasing compound II formation rate, and slowing down the catalase activity rate.

References

[1]  Wang, F., Liu, Y., Du, C. and Gao, R. (2022) Current Strategies for Real-Time Enzyme Activation. Biomolecules, 12, Article 599.
https://doi.org/10.3390/biom12050599
[2]  Bashari, M., Jin, Z., Wang, J. and Zhan, X. (2016) A Novel Technique to Improve the Biodegradation Efficiency of Dextranase Enzyme Using the Synergistic Effects of Ultrasound Combined with Microwave Shock. Innovative Food Science & Emerging Technologies, 35, 125-132.
https://doi.org/10.1016/j.ifset.2016.04.007
[3]  Klyachko, N.L., Sokolsky-Papkov, M., Pothayee, N., Efremova, M.V., Gulin, D.A., Pothayee, N., et al. (2012) Changing the Enzyme Reaction Rate in Magnetic Nanosuspensions by a Non-Heating Magnetic Field. Angewandte Chemie International Edition, 51, 12016-12019.
https://doi.org/10.1002/anie.201205905
[4]  Collins, C.B., Riskowski, R.A. and Ackerson, C.J. (2021) Radiofrequency Remote Control of Thermolysin Activity. Scientific Reports, 11, Article No. 6070.
https://doi.org/10.1038/s41598-021-85611-w
[5]  Veselov, M.M., Uporov, I.V., Efremova, M.V., Le-Deygen, I.M., Prusov, A.N., Shchetinin, I.V., et al. (2022) Modulation of Α-Chymotrypsin Conjugated to Magnetic Nanoparticles by the Non-Heating Low-Frequency Magnetic Field: Molecular Dynamics, Reaction Kinetics, and Spectroscopy Analysis. ACS Omega, 7, 20644-20655.
https://doi.org/10.1021/acsomega.2c00704
[6]  Patruno, A., Tabrez, S., Pesce, M., Shakil, S., Kamal, M.A. and Reale, M. (2015) Effects of Extremely Low Frequency Electromagnetic Field (ELF-EMF) on Catalase, Cytochrome P450 and Nitric Oxide Synthase in Erythro-Leukemic Cells. Life Sciences, 121, 117-123.
https://doi.org/10.1016/j.lfs.2014.12.003
[7]  Blank, M. and Soo, L. (2001) Optimal Frequencies for Magnetic Acceleration of Cytochrome Oxidase and Na,K-ATPase Reactions. Bioelectrochemistry, 53, 171-174.
https://doi.org/10.1016/s0302-4598(00)00128-8
[8]  Glendening, E.D., Landis, C.R. and Weinhold, F. (2019) Resonance Theory Reboot. Journal of the American Chemical Society, 141, 4156-4166.
https://doi.org/10.1021/jacs.8b12336
[9]  Glendening, E.D., Burke, S.D., Moore, J.W. and Weinhold, F. (2022) Physiker versus Organiker Views of Reaction “Mechanism”: How Natural Resonance Theory Bridges the Gap. Journal of Chemical Education, 99, 3702-3712.
https://doi.org/10.1021/acs.jchemed.2c00613
[10]  Glendening, E.D. and Weinhold, F. (2021) Pauling’s Conceptions of Hybridization and Resonance in Modern Quantum Chemistry. Molecules, 26, Article 4110.
https://doi.org/10.3390/molecules26144110
[11]  Messori, C. (2019) Deep into the Water: Exploring the Hydro-Electromagnetic and Quantum-Electrodynamic Properties of Interfacial Water in Living Systems. Open Access Library Journal, 6, e5435.
https://doi.org/10.4236/oalib.1105435
[12]  Davidson, R., Lauritzen, A. and Seneff, S. (2013) Biological Water Dynamics and Entropy: A Biophysical Origin of Cancer and Other Diseases. Entropy, 15, 3822-3876.
https://doi.org/10.3390/e15093822
[13]  Cosic, I., Cosic, D. and Lazar, K. (2015) Is It Possible to Predict Electromagnetic Resonances in Proteins, DNA and RNA? EPJ Nonlinear Biomedical Physics, 3, Article No. 5.
https://doi.org/10.1140/epjnbp/s40366-015-0020-6
[14]  Ikhlov, B.L. (2022) Resonant Absorption of Microwaves by Macromolecules. Open Access Library Journal, 9, e8489.
https://doi.org/10.4236/oalib.1108489
[15]  Chalopin, Y. (2020) The Physical Origin of Rate Promoting Vibrations in Enzymes Revealed by Structural Rigidity. Scientific Reports, 10, Article No. 17465.
https://doi.org/10.1038/s41598-020-74439-5
[16]  Glorieux, C. and Calderon, P.B. (2017) Catalase, a Remarkable Enzyme: Targeting the Oldest Antioxidant Enzyme to Find a New Cancer Treatment Approach. Biological Chemistry, 398, 1095-1108.
https://doi.org/10.1515/hsz-2017-0131
[17]  Góth, L. and Nagy, T. (2013) Inherited Catalase Deficiency: Is It Benign or a Factor in Various Age Related Disorders? Mutation Research/Reviews in Mutation Research, 753, 147-154.
https://doi.org/10.1016/j.mrrev.2013.08.002
[18]  Dasouki, M. (2017) Peroxisomal Disorders. In: Garg, U. and Smith, L.D., Eds., Biomarkers in Inborn Errors of Metabolism, Elsevier, 235-282.
https://doi.org/10.1016/b978-0-12-802896-4.00007-9
[19]  Kirkman, H.N., Rolfo, M., Ferraris, A.M. and Gaetani, G.F. (1999) Mechanisms of Protection of Catalase by NADPH. Journal of Biological Chemistry, 274, 13908-13914.
https://doi.org/10.1074/jbc.274.20.13908
[20]  Murthy, M.R.N., Reid, T.J., Sicignano, A., Tanaka, N. and Rossmann, M.G. (1981) Structure of Beef Liver Catalase. Journal of Molecular Biology, 152, 465-499.
https://doi.org/10.1016/0022-2836(81)90254-0
[21]  Kirkman, H.N. and Gaetani, G.F. (1984) Catalase: A Tetrameric Enzyme with Four Tightly Bound Molecules of NADPH. Proceedings of the National Academy of Sciences, 81, 4343-4347.
https://doi.org/10.1073/pnas.81.14.4343
[22]  Nicholls, P. and Schonbaum, G.R. (1963) Catalases. In: Boyer, P.D., Lardy, H. and Myrback, K., Ed., The Enzymes, Academic Press, 147-225.
[23]  Chance, B. (1950) The Reactions of Catalase in the Presence of the Notatin System. Biochemical Journal, 46, 387-402.
https://doi.org/10.1042/bj0460387
[24]  Nagem, R.A.P., Martins, E.A.L., Gonçalves, V.M., Aparício, R. and Polikarpov, I. (1999) Crystallization and Preliminary X-Ray Diffraction Studies of Human Catalase. Acta Crystallographica Section D Biological Crystallography, 55, 1614-1615.
https://doi.org/10.1107/s0907444999009695
[25]  Zámocký, M. and Koller, F. (1999) Understanding the Structure and Function of Catalases: Clues from Molecular Evolution and in vitro Mutagenesis. Progress in Biophysics and Molecular Biology, 72, 19-66.
https://doi.org/10.1016/s0079-6107(98)00058-3
[26]  Putnam, C.D., Arvai, A.S., Bourne, Y. and Tainer, J.A. (2000) Active and Inhibited Human Catalase Structures: Ligand and NADPH Binding and Catalytic Mechanism. Journal of Molecular Biology, 296, 295-309.
https://doi.org/10.1006/jmbi.1999.3458
[27]  Sugadev, R., Ponnuswamy, M.N. and Sekar, K. (2011) Structural Analysis of NADPH Depleted Bovine Liver Catalase and Its Inhibitor Complexes. International Journal of Biochemistry and Molecular Biology, 2, 67-77.
[28]  Almarsson, O., Sinha, A., Gopinath, E. and Bruice, T.C. (1993) Mechanism of One-Electron Oxidation of NAD(P)H and Function of NADPH Bound to Catalase. Journal of the American Chemical Society, 115, 7093-7102.
https://doi.org/10.1021/ja00069a005
[29]  Gouet, P., Jouve, H. and Dideberg, O. (1995) Crystal Structure of Proteus mirabilispr Catalase with and without Bound NADPH. Journal of Molecular Biology, 249, 933-954.
https://doi.org/10.1006/jmbi.1995.0350
[30]  Gaetani, G.F., Ferraris, A.M., Sanna, P. and Kirkman, H.N. (2005) A Novel NADPH: (Bound) NADP+ Reductase and NADH: (Bound) NADP+ Transhydrogenase Function in Bovine Liver Catalase. Biochemical Journal, 385, 763-768.
https://doi.org/10.1042/bj20041495
[31]  Kaushal, J., Mehandia, S., Singh, G., Raina, A. and Arya, S.K. (2018) Catalase Enzyme: Application in Bioremediation and Food Industry. Biocatalysis and Agricultural Biotechnology, 16, 192-199.
https://doi.org/10.1016/j.bcab.2018.07.035
[32]  Iwase, T., Tajima, A., Sugimoto, S., Okuda, K., Hironaka, I., Kamata, Y., et al. (2013) A Simple Assay for Measuring Catalase Activity: A Visual Approach. Scientific Reports, 3, Article No. 3081.
https://doi.org/10.1038/srep03081
[33]  Maehly, A.C. (1954) The Assay of Catalases and Peroxidases. Methods of Biochemical Analysis, 1, 357-424.
https://doi.org/10.1002/9780470110171.ch14
[34]  Sumner, J.B. and Dounce, A.L. (1937) Crystalline Catalase. Science, 85, 366-367.
https://doi.org/10.1126/science.85.2206.366

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133