Open AccessCharacterization of hydrogenase activities associated with the molybdenum CO dehydrogenase from Oligotropha carboxidovorans
Author(s) -
Santiago Beatrix,
Meyer Ortwin
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08042.x
Subject(s) - hydrogenase , carbon monoxide dehydrogenase , flavin group , molybdenum , dehydrogenase , chemistry , enzyme , cytoplasm , biochemistry , redox , nadh dehydrogenase , photochemistry , inorganic chemistry , catalysis , carbon monoxide , gene , protein subunit
The formation of H 2 by chemolithoautrophically growing Oligotropha carboxidovorans has been identified as the result of the oxidation of CO mediated by the cytoplasmic species of the molybdenum‐containing CO dehydrogenase multienzyme complex as follows: CO + H 2 O → CO 2 + H 2 . Purified CO dehydrogenase was shown to carry hydrogen uptake and formation activities in addition to its catabolic function which is the oxidation of CO. Among the electron donors supporting H 2 formation were CO, NADH, reduced flavins and reduced viologen dyes. The reduction of protons to H 2 by cytoplasmic CO dehydrogenase is interpreted as a detoxification reaction for electrons to prevent cell damage in O. carboxidovorans .