@article {2343,
	title = {A needle in a haystack: the active site of the membrane-bound complex cytochrome c nitrite reductase},
	journal = {FEBS Lett},
	volume = {581},
	number = {2},
	year = {2007},
	note = {<p>0014-5793 (Print)0014-5793 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Jan 23},
	pages = {284-8},
	abstract = {<p>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.</p>
},
	keywords = {Bacterial Proteins/*chemistry/isolation \& purification, Binding Sites, Catalysis, Cytochromes a1/*chemistry/isolation \& purification, Cytochromes c1/*chemistry/isolation \& purification, Desulfovibrio desulfuricans/*enzymology, Heme/*chemistry, Nitrate Reductases/*chemistry/isolation \& purification, Potentiometry, Protons},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=17207484 },
	author = {Almeida, M. G. and Silveira, C. M. and Guigliarelli, B. and Bertrand, P. and Moura, J. J. and Moura, I. and Leger, C.}
}
