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Electrocatalysis at hydrogenase or cytochrorme C 3 ‐modified glassy carbon electrodes
Author(s) -
Bianco Pierre,
Haiadjian Jean
Publication year - 1991
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.1140030915
Subject(s) - hydrogenase , glassy carbon , electrocatalyst , desulfovibrio , chemistry , catalysis , electrochemistry , redox , inorganic chemistry , cytochrome c , carbon fibers , electrode , photochemistry , materials science , sulfate , organic chemistry , cyclic voltammetry , biochemistry , mitochondrion , composite material , composite number
The immobilization of two redox proteins, hydrogenase and cytochrome c 3 extracted from Desulfovibrio desulfurifcans sulfate‐reducing bacterium, on glassy carbon electrodes modified via carbodiimide procedure is reported. The catalytic activity at the hydrogenase‐modified glassy carbon electrode is detected in the presence of methylviologen, which acts as a shuttle between immobilized hydrogenase and the electrode surface. The effect of experimental parameters (e.g., methylviologen concentration or pH) on the catalytic activity is examined; maximum activity is observed at pH 9.5. Catalytic activity is also detected when methylviologen is replaced by cytochrome c 3 , which is the physiological partner of hydrogenase. The cytochrome C 3 ‐modified glassy carbon does not yield a stable electrochemical response due to cytochrome c 3 reconformation at the electrode surface.