The activation of the periplasmic (NiFe) hydrogenase of Desulfovibrio gigas by carbon monoxide

FEBS Letters

Fauque, Guy D.¹  LeGall, Jean¹  Peck, Harry D.²  Lespinat, Paul A.¹  Berlier, Yves M.¹ 

[1] Section Enzymologie et Biochimie Bactérienne, ARBS, CEN Cadarache, 13108 Saint Paul lez Durance Cedex, France;School of Chemical Sciences, Department of Biochemistry, University of Georgia, Athens, GA 30602, USA

关键词: Hydrogenase;    Proton-deuterium exchange;    Enzyme activation;    Carbon monoxide;    (Desulfovibrio gigas);   

DOI  :  10.1016/0014-5793(87)80933-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown