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

26 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
Externally publishedYes

Fingerprint

Cytochromes c
Heme
Electrons
Succinate Dehydrogenase
Polarization
Oxidation-Reduction

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis. / Harada, Erisa; Kumagai, Jiro; Ozawa, Kiyoshi; Imabayashi, Shinichiro; Tsapin, Alexandre S.; Nealson, Kenneth H.; Meyer, Terrance E.; Cusanovich, Michael A.; Akutsu, Hideo.

In: FEBS Letters, Vol. 532, No. 3, 18.12.2002, p. 333-337.

Research output: Contribution to journalArticle

Harada, Erisa ; Kumagai, Jiro ; Ozawa, Kiyoshi ; Imabayashi, Shinichiro ; Tsapin, Alexandre S. ; Nealson, Kenneth H. ; Meyer, Terrance E. ; Cusanovich, Michael A. ; Akutsu, Hideo. / A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis. In: FEBS Letters. 2002 ; Vol. 532, No. 3. pp. 333-337.
@article{eb9df2a5fd0a482a918ad2d6dfc8cc42,
title = "A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis",
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.",
keywords = "Cooperativity, Heme architecture, NMR, Polarography, Redox potential, Tetraheme cytochrome",
author = "Erisa Harada and Jiro Kumagai and Kiyoshi Ozawa and Shinichiro Imabayashi and Tsapin, {Alexandre S.} and Nealson, {Kenneth H.} and Meyer, {Terrance E.} and Cusanovich, {Michael A.} and Hideo Akutsu",
year = "2002",
month = "12",
day = "18",
doi = "10.1016/S0014-5793(02)03696-7",
language = "English",
volume = "532",
pages = "333--337",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis

AU - Harada, Erisa

AU - Kumagai, Jiro

AU - Ozawa, Kiyoshi

AU - Imabayashi, Shinichiro

AU - Tsapin, Alexandre S.

AU - Nealson, Kenneth H.

AU - Meyer, Terrance E.

AU - Cusanovich, Michael A.

AU - Akutsu, Hideo

PY - 2002/12/18

Y1 - 2002/12/18

N2 - 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.

AB - 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.

KW - Cooperativity

KW - Heme architecture

KW - NMR

KW - Polarography

KW - Redox potential

KW - Tetraheme cytochrome

UR - http://www.scopus.com/inward/record.url?scp=0037132498&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037132498&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(02)03696-7

DO - 10.1016/S0014-5793(02)03696-7

M3 - Article

VL - 532

SP - 333

EP - 337

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -