Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity

Ana C. Messias, António P. Aguiar, Lorraine Brennan, Carlos A. Salgueiro, Lígia M. Saraiva, António V. Xavier, David L. Turner

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.

Original languageEnglish
Pages (from-to)143-153
Number of pages11
JournalBiochimica Et Biophysica Acta-Bioenergetics
Volume1757
Issue number2
DOIs
Publication statusPublished - Feb 2006

Keywords

  • Cytochrome c
  • Multihaem cytochromes
  • NMR
  • Redox proteins
  • Tetrahaem cytochrome c

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