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

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)333-337
Number of pages5
JournalFEBS Letters
Volume532
Issue number3
DOIs
Publication statusPublished - 2002 Dec 18

Keywords

  • Cooperativity
  • Heme architecture
  • NMR
  • Polarography
  • Redox potential
  • Tetraheme cytochrome

ASJC Scopus subject areas

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

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    Harada, E., Kumagai, J., Ozawa, K., Imabayashi, S., Tsapin, A. S., Nealson, K. H., Meyer, T. E., Cusanovich, M. A., & Akutsu, H. (2002). A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis. FEBS Letters, 532(3), 333-337. https://doi.org/10.1016/S0014-5793(02)03696-7