Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

Cristina Moreno, Cristina Costa, Isabel MOURA, Jean Le Gall, Ming Y. Liu, William J. Payne, Cees van Dijk, José J. G. Moura

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The electron‐transfer kinetics between three different mediators and the hexahemic enzyme nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774) were investigated by cyclic voltammetry and by chronoamperometry. The mediators, methyl viologen, Desulfovibrio vulgaris (Hildenborough) cytochrome c3 and D. desulfuricans (ATCC 27774) cytochrome c3 differ in structure, redox potential and charge. The reduced form of each mediator exchanged electrons with nitrite reductase. Second‐order rate constants, k, were calculated on the basis of the theory for a simple catalytic mechanism and the results, obtained by cyclic voltammetry, were compared with those obtained by chronoamperometry. Values for k are in the range 106–108 M−1 s−1 and increase in the direction D. desulfuricans cytochrome c3→D. vulgaris cytochrome c3→ methyl viologen. An explanation is advanced on the basis of electrostatic interactions and relative orientation between the partners involved. Chronoamperometry (computer controlled) offers advantages over cyclic voltammetry in the determination of homogeneous rate constants (faster, more accurate and better reproducibility). Direct, unmediated electrochemical responses of the hexaheme nitrite reductase were also reported.

Original languageEnglish
Pages (from-to)79-86
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number1
Publication statusPublished - 1 Jan 1993


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