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Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobactercapsulatus

Nature Structural Biology volume 3, pages 459–464 (1996)Cite this article

Abstract

We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c′. This is the first example of a ligand-bound structure of a class Ha cytochrome c′. Compared with the structure of native cytochrome c′, there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.

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Author notes

  1. Yoshiki Higuchi

    Present address: Division of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-01, Japan

Authors and Affiliations

  1. Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, 678-12, Japan

    Tahir H. Tahirov, Shintaro Misaki, Yoshiki Higuchi & Noritake Yasuoka

  2. Department of Biochemistry, University of Arizona, Tucson, Arizona, 85721, USA

    Terry E. Meyer & Michael A. Cusanovich

  3. Institute of Inorganic and Physical Chemistry, Azerbaijan Academy of Sciences, Husein Javid Prospekti 29, Baku, 370143, Azerbaijan

    Tahir H. Tahirov

Authors
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  2. Shintaro Misaki
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  4. Michael A. Cusanovich
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  5. Yoshiki Higuchi
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  6. Noritake Yasuoka
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Tahirov, T., Misaki, S., Meyer, T. et al. Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobactercapsulatus. Nat Struct Mol Biol 3, 459–464 (1996). https://doi.org/10.1038/nsb0596-459

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