A needle in a haystack: the active site of the membrane-bound complex cytochrome c nitrite reductase
- Citation:
- A needle in a haystack: the active site of the membrane-bound complex cytochrome c nitrite reductase, Almeida, M. G., Silveira C. M., Guigliarelli B., Bertrand P., Moura J. J., Moura I., and Leger C. , FEBS Lett, Jan 23, Volume 581, Number 2, p.284-8, (2007)
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 NrfA2NrfH 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.
Notes:
0014-5793 (Print)0014-5793 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't
