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- Title
A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis
- Authors
Harada, Erisa; Kumagai, Jiro; Ozawa, Kiyoshi; Imabayashi, Shinichiro; Tsapin, Alexandre S.; Nealson, Kenneth H.; Meyer, Terrance E.; Cusanovich, Michael A.; Akutsu, Hideo
- 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.
- Subjects
CYTOCHROME c; SHEWANELLA; OXIDATION-reduction reaction
- Publication
FEBS Letters, 2002, Vol 532, Issue 3, p333
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03696-7