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

Tahir H. Tahirov, Shintaro Misaki, Terry E. Meyer, Michael A. Cusanovich, Yoshiki Higuchi, Noritake Yasuoka

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 IIa 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.

Original languageEnglish (US)
Pages (from-to)459-464
Number of pages6
JournalNature Structural Biology
Volume3
Issue number5
DOIs
StatePublished - Jan 1 1996

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Rhodobacter capsulatus
Cytochromes c
Heme
Ligands
Proton transfer
Propionates
Hydrogen Bonding
Dimers
Protons
Hydrogen bonds
Amino Acids

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Cite this

Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobacter capsulatus. / Tahirov, Tahir H.; Misaki, Shintaro; Meyer, Terry E.; Cusanovich, Michael A.; Higuchi, Yoshiki; Yasuoka, Noritake.

In: Nature Structural Biology, Vol. 3, No. 5, 01.01.1996, p. 459-464.

Research output: Contribution to journalArticle

Tahirov, Tahir H. ; Misaki, Shintaro ; Meyer, Terry E. ; Cusanovich, Michael A. ; Higuchi, Yoshiki ; Yasuoka, Noritake. / Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobacter capsulatus. In: Nature Structural Biology. 1996 ; Vol. 3, No. 5. pp. 459-464.
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