1994
DOI: 10.1016/0300-9084(94)90177-5
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A detailed comparison of the refined structures of cytochrome c3 molecules from two strains in Desulfovibrio vulgaris: The relationship between the heme structure and their redox properties

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Cited by 8 publications

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“…A large number of multihaem cytochromes with different haem contents, varying from three to 16 haem groups per polypeptide chain, are currently known. The crystal structures of tetrahaem (Czjzek, Payan, Guerlesquin et al, 1994;Haser, Pierrot et al, 1979;Higuchi et al, 1984Higuchi et al, , 1994Matias et al, 1993Matias et al, , 1996Nùrager et al, 1999), octahaem (Czjzek et al, 1996, Fraza Ä o et al, 1999 and nonahaem (Matias et al, 1999) cytochromes c 3 demonstrate that these proteins are variants and/or multimers of the tetrahaem cytochrome c 3 motif. The recently obtained NMR solution structure of cytochrome c 7 (Assfalg et al, 1998) revealed that this cytochrome is no exception and, as has been predicted by sequence alignments, it is the haem 2 and the corresponding protein chain that are missing in this shortest version of cytochromes c 3 .…”
Section: Introduction
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confidence: 99%