A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis

Erisa Harada, Jiro Kumagai, Kiyoshi Ozawa, Shinichiro Imabayashi, Alexandre S. Tsapin, Kenneth H. Nealson, Terrance E. Meyer, Michael A. Cusanovich, Hideo Akutsu

研究成果: Article査読

32 被引用数 (Scopus)

抄録

The macroscopic and microscopic redox potentials of the four hemes of the small tetraheme cytochrome c from Shewanella oneidensis were determined. The microscopic redox potentials show that the order of reduction is from hemes in the C-terminal domain (hemes 3 and 4) to the N-terminal domain (heme 1), demonstrating the polarization of the tetraheme chain during reduction. This makes heme 4 the most efficient electron delivery site. Furthermore, multi-step reduction of other redox centers through either heme 4 or heme 3 is shown to be possible. This has provided new insights into the two-electron reduction of the flavin in the homologous flavocytochrome c-fumarate reductase.

本文言語English
ページ(範囲)333-337
ページ数5
ジャーナルFEBS Letters
532
3
DOI
出版ステータスPublished - 2002 12 18
外部発表はい

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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