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• W2079497282 abstract "Cytochrome P 450nor ( P 450nor) is a heme‐containing nitric oxide reductase from the denitrifying fungus, Fusarium oxysporum . This enzyme catalyzes the reduction of NO to N 2 O. In the present study, we report results from preliminary crystallographic and electron paramagnetic resonance (EPR) analysis of a single crystal of P 450nor. The crystal was grown in 100 mM MES buffer at pH 5.6 using PEG 4000 as a precipitant. It belongs to the orthorhombic system with cell dimensions of a =54.99 Å, b =82.66 Å, c =87.21 Å, and the space group is P 2 1 2 1 2 1 . The crystal diffracts synchrotron radiation at higher than 2.0 Å resolution, and therefore it is suitable for X‐ray crystal structure analysis at atomic resolution. Bijvoet and dispersive anomalous difference Patterson maps show a clear peak corresponding to the heme iron. The structure solution is currently underway by means of MIR and MAD techniques. EPR analysis determined the orientation of the heme within the P 450nor crystal." @default.
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• W2079497282 date "1997-07-28" @default.
• W2079497282 modified "2023-10-03" @default.
• W2079497282 title "Crystallization, preliminary diffraction and electron paramagnetic resonance studies of a single crystal of cytochrome<i>P</i>450nor" @default.
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• W2079497282 doi "https://doi.org/10.1016/s0014-5793(97)00795-3" @default.
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