Abstract
The modified pyrolytic graphite electrode resulting from the adsorption of hydrogenase from Desulfovibrio desulfuricans Norway on the graphite surface is used to study the interaction between hydrogenase and its physiological redox partner cytochrome c 3. The kinetics of the system hydrogenase/cytochrome c 3 are investigated using cyclic voltammetry. It is shown that the catalytic current depends on several factors such as the ionic strength and pH. By varying the cytochrome c 3 concentration a value of 3 μM is obtained for the “apparent” Michaelis-Menten constant. The comparison with other cytochromes c 3 shows that a poor current is detected for the system Desulfovibrio desulfuricans Norway hydrogenase/ Desulfovibrio gigas cytochrome c 3.
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