Etude des activités NADH et NADPH-ferrédoxine oxydoréductasiques chez Clostridium acetobutylicum
- 1 February 1977
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 23 (2) , 152-160
- https://doi.org/10.1139/m77-022
Abstract
The NADH and NADPH-ferredoxin oxidoreductase were studied in C. acetobutylicum. Acetyl-CoA is an obligatory activator of NADH-ferredoxin reductase activity and NADH a competitive inhibitor of ferredoxin-NAD+ reductase activity. These regulations are the same when C. acetobutylicum moves from butylic-type metabolism to butyric-type metabolism; this demonstrates that NADH-ferredoxin oxidoreductase can, through its reversible action, meet the very different cell needs imposed by these 2 types of culture. The physiological function of the clostridial NADPH-ferredoxin oxidoreductase was anabolic as it is with other clostridia.This publication has 7 references indexed in Scilit:
- Purification and analysis of ferredoxin from Clostridium pasteurianumBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- Studies on the Chemical Nature of Clostridial FerredoxinJournal of Biological Chemistry, 1963
- ROLE OF FERREDOXIN IN PYRIDINE NUCLEOTIDE REDUCTIONProceedings of the National Academy of Sciences, 1962
- THE OXIDATION OF ACETALDEHYDE TO ACETYL COENZYME AJournal of Biological Chemistry, 1953
- COENZYME A FUNCTION IN AND ACETYL TRANSFER BY THE PHOSPHOTRANSACETYLASE SYSTEMJournal of Biological Chemistry, 1951
- *RECUPERATION DE LA PENICILLINE DANS LES URINES1945
- Studies on the acetone-butyl alcohol fermentationBiochemical Journal, 1941