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Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
Published on: April 16, 2018
A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from
Erisa Harada1, Jiro Kumagai, Kiyoshi Ozawa
1Institute for Protein Research, Osaka University, Yamadaoka, Suita, 565-0871, Osaka, Japan.
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.
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