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PMID:9095195
| Citation |
Igarashi, N, Moriyama, H, Fujiwara, T, Fukumori, Y and Tanaka, N (1997) The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nat. Struct. Biol. 4:276-84 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Computer Simulation; Crystallography, X-Ray; Electron Transport; Heme/analogs & derivatives; Heme/chemistry; Hydroxylamine; Hydroxylamines/metabolism; Models, Molecular; Molecular Sequence Data; Nitrosomonas/enzymology; Oxidoreductases/chemistry; Protein Conformation; Software; Surface Properties |
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