Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase

The reaction between cytochrome c(Cc) and Rhodobacter sphaeroides cytochrome coxidase (CcO) was studied using a cytochrome c derivative labeled with ruthenium trisbipyridine at lysine 55 (Ru-55-Cc). Flash photolysis of a 1:1 complex between Ru-55-Cc and CcO at low ionic strength results in electron transfer from photoreduced heme c to CuA with an intracomplex rate constant ofk a = 4 × 104 s−1, followed by electron transfer from CuA to heme a with a rate constant of k b = 9 × 104s−1. The effects of CcO surface mutations on the kinetics follow the order D214N > E157Q > E148Q > D195N > D151N/E152Q ≈ D188N/E189Q ≈ wild type, indicating that the acidic residues Asp214, Glu157, Glu148, and Asp195 on subunit II interact electrostatically with the lysines surrounding the heme crevice of Cc. Mutating the highly conserved tryptophan residue, Trp143, to Phe or Ala decreased the intracomplex electron transfer rate constant k a by 450- and 1200-fold, respectively, without affecting the dissociation constant K D . It therefore appears that the indole ring of Trp143 mediates electron transfer from the heme group of Cc to CuA. These results are consistent with steady-state kinetic results (Zhen, Y., Hoganson, C. W., Babcock, G. T., and Ferguson-Miller, S. (1999) J. Biol. Chem. 274, 38032–38041) and a computational docking analysis (Roberts, V. A., and Pique, M. E. (1999) J. Biol. Chem.274, 38051–38060).

• Publication year

  1999

• Venue

  Journal of Biological Chemistry

• Publication date

  1999-12-31

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/jbc.274.53.38042PMID 10608873
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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