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 H(2) 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.
Cordas
Cristina M
CM
REQUIMTE - Departamento de Química, CQFB, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2859-516 Monte de Caparica, Portugal.
Moura
Isabel
I
Moura
José J G
JJ
D001426:Bacterial Proteins; D045286:Desulfovibrio gigas / Q000201:enzymology*; D004563:Electrochemistry; D004566:Electrodes; D004789:Enzyme Activation; D006859:Hydrogen / Q000737:chemistry; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007501:Iron; D009532:Nickel; D010084:Oxidation-Reduction
D001426:Bacterial Proteins; D009532:Nickel; D006859:Hydrogen; D007501:Iron; C043296:nickel-iron hydrogenase; D006864:Hydrogenase