Direct voltammetry of the Chromatium vinosum enzyme, sulfide:cytochrome c oxidoreductase (flavocytochrome c552).
The electrochemistry of the enzyme, sulfide:cytochrome c oxidoreductase, also known as flavocytochrome c552 from the purple sulfur bacterium, Chromatium vinosum, has been studied using several modified electrodes. Direct electron transfer between the heme of the flavocytochrome and an electrode is observed in the presence of a redox-inactive cationic species which promotes the voltammetry of the enzyme. Quasi-reversible electron transfer was achieved using the aminoglycoside, neomycin, as a promoter at either a modified gold or polished edge-plane graphite electrode. Further evidence for direct electron transfer is provided by the catalytic response of the enzyme at the electrode in the presence of substrate. Also reported is the direct spectroelectrochemistry of flavocytochrome c552 at an optically transparent thin layer gold electrode modified with Cys-Glu-Cys in the presence of neomycin.
Guo
L H
LH
Inorganic Chemistry Laboratory, Oxford, United Kingdom.
Hill
H A
HA
Hopper
D J
DJ
Lawrance
G A
GA
Sanghera
G S
GS
D002844:Chromatium / Q000201:enzymology*; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D007700:Kinetics; D009355:Neomycin / Q000494:pharmacology; D011199:Potentiometry / Q000379:methods
D003574:Cytochrome c Group; C083951:cytochrome c553; C022302:cytochrome C-552; D009355:Neomycin