The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3)

Sulfate-reducing bacteria contain a variety of multi-heme c-type cytochromes. The cytochrome of highest molecular weight (Hmc) contains 16 heme groups and is part of a transmembrane complex involved in the sulfate respiration pathway. We present the 2.42 A resolution crystal structure of the Desulfo...

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Bibliographic Details
Published in:Structure (London) 2002-12, Vol.10 (12), p.1677-1686
Main Authors: Czjzek, Mirjam, ElAntak, Latifa, Zamboni, Véronique, Morelli, Xavier, Dolla, Alain, Guerlesquin, Françoise, Bruschi, Mireille
Format: Article
Language:English
Subjects:
Crystallography, X-Ray
Cytochromes - chemistry
Heme - chemistry
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
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Summary:Sulfate-reducing bacteria contain a variety of multi-heme c-type cytochromes. The cytochrome of highest molecular weight (Hmc) contains 16 heme groups and is part of a transmembrane complex involved in the sulfate respiration pathway. We present the 2.42 A resolution crystal structure of the Desulfovibrio vulgaris Hildenborough cytochrome Hmc and a structural model of the complex with its physiological electron transfer partner, cytochrome c(3), obtained by NMR restrained soft-docking calculations. The Hmc is composed of three domains, which exist independently in different sulfate-reducing species, namely cytochrome c(3), cytochrome c(7), and Hcc. The complex involves the last heme at the C-terminal region of the V-shaped Hmc and heme 4 of cytochrome c(3), and represents an example for specific cytochrome-cytochrome interaction.
ISSN:0969-2126
DOI:10.1016/S0969-2126(02)00909-7