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A. Pearson, Bradley Elmore, Cheng Yang, J. Ferrara, A. Hooper, C. Wilmot (2007)
The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.Biochemistry, 46 28
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The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaeaNature Structural Biology, 4
Hydroxylamine oxidoreductase (HAO) from Nitrosomonas europaea is a homotrimeric protein that catalyzes the oxidation of hydroxylamine to nitrite. Each monomer, with a molecular weight of 67.1 kDa, contains seven c‐type hemes and one heme P460, the porphyrin ring of which is covalently linked to a tyrosine residue from an adjacent subunit. HAO was first crystallized and structurally characterized at a resolution of 2.8 Å in 1997. The structure was solved in space group P63 and suffered from merohedral twinning. Here, a crystallization procedure is presented that yielded untwinned crystals belonging to space group P21212, which diffracted to 2.25 Å resolution and contained one trimer in the asymmetric unit. The unit‐cell parameters were a = 140.7, b = 142.6, c = 107.4 Å.
Acta Crystallographica Section F – Wiley
Published: Dec 1, 2009
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