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- W2082027006 abstract "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 Å resolution crystal structure of the Desulfovibrio vulgaris Hildenborough cytochrome Hmc and a structural model of the complex with its physiological electron transfer partner, cytochrome c3, obtained by NMR restrained soft-docking calculations. The Hmc is composed of three domains, which exist independently in different sulfate-reducing species, namely cytochrome c3, cytochrome c7, and Hcc. The complex involves the last heme at the C-terminal region of the V-shaped Hmc and heme 4 of cytochrome c3, and represents an example for specific cytochrome-cytochrome interaction." @default.
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- W2082027006 date "2002-12-01" @default.
- W2082027006 modified "2023-09-30" @default.
- W2082027006 title "The Crystal Structure of the Hexadeca-Heme Cytochrome Hmc and a Structural Model of Its Complex with Cytochrome c3" @default.
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- W2082027006 doi "https://doi.org/10.1016/s0969-2126(02)00909-7" @default.
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