Your browser version may not work well with NCBI's Web applications. More information here...
1: Nat Struct Biol. 1997 Apr;4(4):276-84.Links
Comment in:
Nat Struct Biol. 1997 Apr;4(4):247-50.
Nat Struct Biol. 1997 Apr;4(4):262.

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

Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N.

Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.

The 2.8 A 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.

PMID: 9095195 [PubMed - indexed for MEDLINE]

Structures reported by this article