%0 Journal Article
%T Structure-Function Relations in Oxaloacetate Decarboxylase Complex. Fluorescence and Infrared Approaches to Monitor Oxomalonate and Na+ Binding Effect
%A Thierry Granjon
%A Ofelia Maniti
%A Yolanda Auchli
%A Pius Dahinden
%A Ren¨¦ Buchet
%A Olivier Marcillat
%A Peter Dimroth
%J PLOS ONE
%D 2012
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0010935
%X Oxaloacetate decarboxylase (OAD) is a member of the Na+ transport decarboxylase enzyme family found exclusively in anaerobic bacteria. OAD of Vibrio cholerae catalyses a key step in citrate fermentation, converting the chemical energy of the decarboxylation reaction into an electrochemical gradient of Na+ ions across the membrane, which drives endergonic membrane reactions such as ATP synthesis, transport and motility. OAD is a membrane-bound enzyme composed of ¦Á, ¦Â and ¦Ã subunits. The ¦Á subunit contains the carboxyltransferase catalytic site.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0010935