Structural basis of inter-protein electron transfer for nitrite reduction in denitrification

Masaki Nojiri (), Hiroyasu Koteishi, Takuya Nakagami, Kazuo Kobayashi, Tsuyoshi Inoue, Kazuya Yamaguchi and Shinnichiro Suzuki ()
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Masaki Nojiri: Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
Hiroyasu Koteishi: Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
Takuya Nakagami: Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
Kazuo Kobayashi: The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan
Tsuyoshi Inoue: Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan
Kazuya Yamaguchi: Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan
Shinnichiro Suzuki: Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan

Nature, 2009, vol. 462, issue 7269, 117-120

Abstract: Interprotein electron transfer in denitrification Nitrous oxide (N2O) is a greenhouse gas that is an intermediate during the biological process known as 'denitrification'. Copper-containing nitrite reductase (CuNIR) produces a precursor for N2O by catalysing the one-electron reduction of nitrite to nitric oxide. This reduction step is specifically regulated by an efficient electron-transfer reaction with a redox-partner protein. In this study, Nojiri et al. report the high-resolution crystal structure of the electron-transfer complex for CuNIR with its cognate cytochrome c as the electron donor. The hydrophobic electron-transfer path is formed at the docking interface of two proteins.

Date: 2009
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DOI: 10.1038/nature08507

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