A needle in a haystack: The active site of the membrane-bound complex cytochrome c nitrite reductase

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Abstract

Cytochrome c nitrite reductase is a multicenter enzyme that uses a five-coordinated heme to perform the six-electron reduction of nitrite to ammonium. In the sulfate reducing bacterium Desulfovibrio desulfuricans ATCC 27774, the enzyme is purified as a NrfA(2)NrfH complex that houses 14 hemes. The number of closely-spaced hemes in this enzyme and the magnetic interactions between them make it very difficult to study the active site by using traditional spectroscopic approaches such as EPR or UV-Vis. Here, we use both catalytic and non-catalytic protein film voltammetry to simply and unambiguously determine the reduction potential of the catalytic heme over a wide range of pH and we demonstrate that proton transfer is coupled to electron transfer at the active site. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageUnknown
Pages (from-to)284-288
JournalFEBS Letters
Volume581
Issue number2
DOIs
Publication statusPublished - 1 Jan 2007

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