The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea

Noriyuki Igarashi, Hideaki Moriyama, Taketomo Fujiwara, Yoshihiro Fukumori, Nobuo Tanaka

Research output: Contribution to journalArticlepeer-review

187 Scopus citations

Abstract

The 2.8 Å crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations.

Original languageEnglish (US)
Pages (from-to)276-284
Number of pages9
JournalNature Structural Biology
Volume4
Issue number4
DOIs
StatePublished - Apr 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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