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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Masaki Nojiri & Hiroyasu Koteishi & Takuya Nakagami & Kazuo Kobayashi & Tsuyoshi Inoue & Kazuya Yamaguchi & Shinnichiro Suzuki, 2009. "Structural basis of inter-protein electron transfer for nitrite reduction in denitrification," Nature, Nature, vol. 462(7269), pages 117-120, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7269:d:10.1038_nature08507
    DOI: 10.1038/nature08507
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