An Intermediate Conformational State during Ligand Binding to Cytochrome <i>c</i> Oxidase Detected by Time-resolved Resonance Raman Analyses of Heme Peripheral Groups

• Izumi Ishigami

  Department of Life Science, Graduate School of Life Science, University of Hyogo

• Takeshi Nishigaki

  Department of Life Science, Graduate School of Life Science, University of Hyogo

• Kyoko Shinzawa-Itoh

  Department of Life Science, Graduate School of Life Science, University of Hyogo

• Shinya Yoshikawa

  Department of Life Science, Graduate School of Life Science, University of Hyogo

• Satoru Nakashima

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

• Takashi Ogura

  Department of Life Science, Graduate School of Life Science, University of Hyogo

抄録

A time-resolved resonance Raman analysis shows that the vinyl stretching band (1629 cm−1) of the O2-binding heme of cytochrome c oxidase shifts to 1627 cm−1 instantaneously upon photolysis of CO and remains for at least 5 ms before reaching the static band (1626 cm−1). Within the same time scale, an intermediate vinyl bending mode of another heme appears at 435 cm−1. These results suggest that both hemes cooperatively control O2 binding by forming an intermediate conformation for effective proton pumping.

収録刊行物

• Chemistry Letters

  Chemistry Letters 41 (2), 178-180, 2012-02

  Oxford University Press (OUP)

キーワード

• General Chemistry

詳細情報

• CRID: 1360565169065085440
• NII論文ID: 130004426495
• DOI: 10.1246/cl.2012.178
• ISSN: 13480715
• ISSN: 03667022
• Web Site: https://academic.oup.com/chemlett/article-pdf/41/2/178/55641450/cl.2012.178.pdf
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