Premium
The activation of the periplasmic (NiFe) hydrogenase of Desulfovibrio gigas by carbon monoxide
Author(s) -
Berlier Yves M.,
Fauque Guy D.,
LeGall Jean,
Lespinat Paul A.,
Peck Harry D.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80933-x
Subject(s) - hydrogenase , periplasmic space , carbon monoxide , chemistry , dithionite , desulfovibrio , redox , inorganic chemistry , hydrogen , enzyme , catalysis , biochemistry , organic chemistry , escherichia coli , sulfate , gene
The activation of the periplasmic (NiFe) hydrogenase from Desulfovibrio gigas by dihydrogen is a complex phenomenon involving both ‘slow’ and ‘fast’ reactions. Carbon monoxide, a competitive inhibitor of hydrogenase activity, is demonstrated to cause the slow activation nearly as well as dihydrogen. Carbon monoxide does not reduce the (NiFe) hydrogenase and the fast reductive activation is effected by deuterium in the exchange assay. In the presence of dithionite, which immediately reduces the redox centers of the (NiFe) hydrogenase, the slow activation is still essential to attain full activity. Thus, the slow non‐reductive and fast reductive steps of the activation can occur in any sequence.