Direct electrochemical study of the multiple redox centers of hydrogenase from Desulfovibrio gigas

Direct electrochemical response was first time observed for the redox centers of Desulfovibrio gigas [NiFe]-Hase, in non-turnover conditions, by cyclic voltammetry, in solution at glassy carbon electrode. The activation of the enzyme was achieved by reduction with H2 and by electrochemical control a...

Full description

Saved in:
Bibliographic Details
Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2008-11, Vol.74 (1), p.83-89
Main Authors: Cordas, Cristina M., Moura, Isabel, Moura, José J.G.
Format: Article
Language:English
Subjects:
Activation
Bacterial Proteins
Biocatalysis
Desulfovibrio gigas
Desulfovibrio gigas - enzymology
Electrochemistry
Electrodes
Enzyme Activation
Hydrogen - chemistry
Hydrogenase - chemistry
Hydrogenase - metabolism
Hydrogenases
Iron
Marine
Nickel
Oxidation-Reduction
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Direct electrochemical response was first time observed for the redox centers of Desulfovibrio gigas [NiFe]-Hase, in non-turnover conditions, by cyclic voltammetry, in solution at glassy carbon electrode. The activation of the enzyme was achieved by reduction with H2 and by electrochemical control and electrocatalytic activity was observed. The inactivation of the [NiFe]-Hase was also attained through potential control. All electrochemical data was obtained in the absence of enzyme inhibitors. The results are discussed in the context of the proposed mechanism currently accepted for activation/inactivation of [NiFe]-Hases.
ISSN:1567-5394
1878-562X
DOI:10.1016/j.bioelechem.2008.04.019