Open AccessÉtude du système multienzymatique hydrogène lyase chez Escherichia coli K 12 et ses mutants chlorate‐résistants
Author(s) -
Azoulay Edgard,
Marty Bernard
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00914.x
Subject(s) - formate dehydrogenase , formate , chlorate , escherichia coli , chemistry , electron acceptor , biochemistry , dehydrogenase , enzyme , hydrogenase , mutant , nitrate reductase , photochemistry , nuclear chemistry , inorganic chemistry , catalysis , gene
The hydrogen lyase system of Escherichia coli K12 which decomposed formate to hydrogen and carbon dioxide involves two particulate enzymes, formate dehydrogenase and hydrogenase, and a soluble component. Formate dehydrogenase, as measured using phenazine methosulfate as electron acceptor, has been localized in particles bearing nitrate reductase activity. Formate dehydrogenase is synthesized throughout anaerobic growth and is not repressed by KNO 3 . This behavior is unlike that of the soluble fraction which does not appear until the end of exponential growth and which can only be considered as an electron carrier. Particulate preparations from cells of the E. coli K12 pleotropic mutants chl A − and chl B − do not have formic dehydrogenase activity, but if the supernatants of these same cells are added to particulate fractions of the wild type, the mixture produces H 2 from formate. These results agree with our earlier observations suggesting that these pleiotropic mutations affect particle structure.