Direct electrochemistry of a bacterial sulfite dehydrogenase

Aguey-Zinsou, Kondo-Francois, Bernhardt, Paul. V., Kappler, Ulrike and McEwan, Alastair G. (2003) Direct electrochemistry of a bacterial sulfite dehydrogenase. Journal of The American Chemical Society, 125 2: 530-535. doi:10.1021/ja028293e


Author Aguey-Zinsou, Kondo-Francois
Bernhardt, Paul. V.
Kappler, Ulrike
McEwan, Alastair G.
Title Direct electrochemistry of a bacterial sulfite dehydrogenase
Journal name Journal of The American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
Publication date 2003-01-01
Year available 2003
Sub-type Article (original research)
DOI 10.1021/ja028293e
Open Access Status Not yet assessed
Volume 125
Issue 2
Start page 530
End page 535
Total pages 6
Place of publication Washington, D.C.
Publisher American Chemical Society
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
Abstract Sulfite dehydrogenase from Starkeya novella is an alphabeta heterodimer comprising a 40.6 kDa subunit (containing the Mo cofactor) and a smaller 8.8 kDa heme c subunit. The enzyme catalyses the oxidation of sulfite to sulfate with the natural electron acceptor being cytochrome c(550). Its catalytic mechanism is thought to resemble that found in eukaryotic sulfite oxiclases. Using protein film voltammetry and redox potentiometry, we have identified both Mo- and heme-centered redox responses from the enzyme immobilized on a pyrolytic graphite working electrode: E-m,E-8 (Fe-III/II) +177 mV; E-m,E-8 (Mo-VI/V) +211 mV and E(m,)8 (Mo-V/IV) -118 mV vs NHE; Upon addition of sulfite to the electrochemical cell a steady-state voltammogram is observed and an apparent Michaelis constant (K-m) of 26(l) muM was determined for the enzyme immobilized on the working electrode surface, which is comparable with the value obtained from solution assays.
Keyword Chemistry, Multidisciplinary
Mononuclear Molybdenum Enzymes
Ray-absorption Spectroscopy
Electron-transfer
Chicken Liver
Molecular-biology
Cytochrome-c
Active-site
High Ph
Oxidase
Biosensor
Q-Index Code C1
Institutional Status UQ

 
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Created: Wed, 15 Aug 2007, 11:34:19 EST