The activation of the periplasmic (NiFe) hydrogenase of Desulfovibrio gigas by carbon monoxide
- 14 September 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 221 (2) , 241-244
- https://doi.org/10.1016/0014-5793(87)80933-x
Abstract
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.Keywords
This publication has 14 references indexed in Scilit:
- Proton-tritium exchange activity of activated and deactivated forms of Desulfovibrio gigas hydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- ESR-detectable nickel and iron-sulphur centres in relation to the reversible activation of Desulfovibrio gigas hydrogenaseBiochimica et Biophysica Acta (BBA) - General Subjects, 1986
- EPR evidence for direct interaction of carbon monoxide with nickel in hydrogenase from Chromatium vinosumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Activation and active sites of nickel-containing hydrogenasesBiochimie, 1986
- Properties and reactivation of two different deactivated forms of Desulfovibrio gigas hydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Direct Mass-Spectrometric Monitoring of the Metabolism and Isotope Exchange in Enzymic and Microbiological InvestigationsPublished by Springer Nature ,1985
- Activation, reduction and proton—deuterium exchange reaction of the periplasmic hydrogenase from Desulfovibrio gigas in relation with the role of cytochrome c3FEBS Letters, 1982
- Inactivation of Hydrogenase in Cell-free Extracts and Whole Cells of Chlamydomonas reinhardi by OxygenPlant Physiology, 1979
- Characterization of the periplasmic hydrogenase from Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1978
- Colorimetric determination of trace levels of oxygen in gases with the photochemically generated methyl viologen radical-cationAnalytical Chemistry, 1967