Cooperation of Two Quinone-Binding Sites in the Oxidation of Substrates by Cytochrome bo

  • Mariko Sato-Watanabe
  • Tatsushi Mogi
  • Hideto Miyoshi
  • Yasuhiro Anraku
Conference paper
Part of the Keio University Symposia for Life Science and Medicine book series (KEIO, volume 1)

Summary

Cytochrome bo is a terminal quinol oxidase of the aerobic respiratory chain of Escherichia coli and catalyzes not only the scalar protolytic reactions but also redox-coupled proton pumping. Structure-function studies of the quinol oxidation site (QL) using systematically selected quinone analogues, 1,4-benzoquinones, substituted phenols, and ubiquinone-2 derivatives revealed the structural features of the quinol oxidation site. We found further that bacterial quinol oxidases share common features of the quinol oxidation site irrespective of their structural similarities. In addition, we identified the presence of a tightly bound ubiquinone-8 (QH) and examined the possible roles of the QH site in the two-electron oxidation of substrates at the QL site and in mediating sequential one-electron transfer from QL to the low-spin heme b. Based on these observations, we discuss molecular mechanism of the substrate oxidation by cytochrome bo.

Key words

Cytochrome bo Intramolecular electron transfer Semiquinone radical Quinol oxidation site Quinone analogues 
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Copyright information

© Springer-Verlag Tokyo 1998

Authors and Affiliations

  • Mariko Sato-Watanabe
    • 1
  • Tatsushi Mogi
    • 1
  • Hideto Miyoshi
    • 2
  • Yasuhiro Anraku
    • 1
  1. 1.Department of Biological Sciences, Graduate School of ScienceUniversity of TokyoBunkyo-ku, Tokyo 113Japan
  2. 2.Department of Agricultural ChemistryKyoto UniversitySakyo-ku, Kyoto 606Japan

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