Stepwise Binding of Two Azide Ions to the O2-reduction Site of Bovine Heart Cytochrome <i>c</i> Oxidase Shown by Resonance Raman Analyses

• Masahide Hikita

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

• Akima Yamamoto

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

• Kyoko Shinzawa-Itoh

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

• Takashi Ogura

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

• Shinya Yoshikawa

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

Abstract

In efforts to probe the function of the O2-reduction site of bovine heart resting oxidized cytochrome c oxidase, highly sensitive resonance Raman analyses of azide binding to the O2-reduction site show that azide is simultaneously accessible to Fe and Cu ions in the O2-reduction site. This indicates that the site has spatial multiplicity for accepting significantly larger external ligands than expected from its X-ray structure. This could contribute to the accurate coupling between the O2 reduction and the proton pump.

Journal

• Chemistry Letters

  Chemistry Letters 44 (8), 1142-1144, 2015-08

  Oxford University Press (OUP)

Keywords

• General Chemistry

Details

• CRID: 1360565169059113472
• NII Article ID: 130005092608
• DOI: 10.1246/cl.150384
• ISSN: 13480715
• ISSN: 03667022
• Web Site: https://academic.oup.com/chemlett/article-pdf/44/8/1142/55644572/cl.150384.pdf
• Data Source:
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