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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/1656

Title: Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase
Authors: Moura, Isabel
Santos, Margarida M. Correia dos
Sousa, Patrícia M. P.
Gonçalves, M. Lurdes S.
Romão, M. João
Moura, José J. G.
Keywords: Aldehyde oxidoreductase
Desulfovibrio gigas
Electrochemistry
Issue Date: 2004
Publisher: Blackwell Publishing
Abstract: This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox-active cofactors: two [2Fe-2S] centers and a molybdopterin cytosine dinucleotide cofactor. The voltammetric behavior of the enzyme was analyzed at gold and carbon (pyrolytic graphite and glassy carbon) electrodes. Two different strategies were used: one with the molecules confined to the electrode surface and a second with DgAOR in solution. In all of the cases studied, electron transfer took place, although different redox reactions were responsible for the voltammetric signal. From a thorough analysis of the voltammetric responses and the structural properties of the molecular surface of DgAOR, the redox reaction at the carbon electrodes could be assigned to the reduction of the more exposed iron cluster, [2Fe-2S] II, whereas reduction of the molybdopterin cofactor occurs at the gold electrode. Voltammetric results in the presence of aldehydes are also reported and discussed.
Description: Eur. J. Biochem. 271, 1329–1338 (2004)
URI: http://hdl.handle.net/10362/1656
ISSN: 00142956
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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