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Crystal structures of the nitric oxide reductase cytochrome P450nor in the ferric resting and the ferrous carbonmonoxy (CO) states have been determined at 1.00 and 1.05 Å resolution, respectively.

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Crystallization and preliminary crystallographic study of cytochrome P450 from B. subtilis, which catalyzes hydroxylation of long-chain fatty acids at the α and β positions using H2O2 as an oxidant, is reported.
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