Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris
Cytochrome P450 enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. Cytochrome P450 203A1 (CYP203A1, RPA1009) from the metabolically versatile organism Rhodopseudomonas palustris binds a broad range of...
المؤلفون الرئيسيون: | Pang, X, Xu, F, Bell, S, Guo, D, Wong, L, Rao, Z |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2007
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مواد مشابهة
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Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.
حسب: Pang, X, وآخرون
منشور في: (2007) -
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris.
حسب: Bell, S, وآخرون
منشور في: (2006) -
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris.
حسب: Bell, S, وآخرون
منشور في: (2008) -
Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.
حسب: Peng, Y, وآخرون
منشور في: (2007) -
Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris.
حسب: Bell, S, وآخرون
منشور في: (2010)