| Literature DB >> 9095195 |
N Igarashi1, H Moriyama, T Fujiwara, Y Fukumori, N Tanaka.
Abstract
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.Entities:
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Year: 1997 PMID： 9095195 DOI： 10.1038/nsb0497-276
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368