@article {2553,
	title = {Mossbauer characterization of the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Spectral deconvolution of the heme components},
	journal = {Eur J Biochem},
	volume = {204},
	number = {2},
	year = {1992},
	note = {<p>0014-2956 (Print)0014-2956 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.Research Support, U.S. Gov{\textquoteright}t, P.H.S.</p>
},
	month = {Mar 1},
	pages = {779-82},
	abstract = {<p>Mossbauer spectroscopy was used to study the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Samples with different degrees of reduction were prepared using a redoxtitration technique. In the reduced cytochrome c3, all four hemes are reduced and exhibit diamagnetic Mossbauer spectra typical for low-spin ferrous hemes (S = 0). In the oxidized protein, the hemes are low-spin ferric (S = 1/2) and exhibit overlapping magnetic Mossbauer spectra. A method of differential spectroscopy was applied to deconvolute the four overlapping heme spectra and a crystal-field model was used for data analysis. Characteristic Mossbauer spectral components for each heme group are obtained. Hyperfine and crystal-field parameters for all four hemes are determined from these deconvoluted spectra.</p>
},
	keywords = {Cytochrome c Group/*chemistry, Desulfovibrio/*enzymology, Heme/chemistry, Oxidation-Reduction, Protein Conformation, Spectroscopy, Mossbauer},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=1311680 },
	author = {Ravi, N. and Moura, I. and Costa, C. and Teixeira, M. and Legall, J. and Moura, J. J. and Huynh, B. H.}
}
