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...
Huvudupphovsmän: | Pang, X, Xu, F, Bell, S, Guo, D, Wong, L, Rao, Z |
---|---|
Materialtyp: | Journal article |
Språk: | English |
Publicerad: |
2007
|
Liknande verk
Liknande verk
-
Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.
av: Pang, X, et al.
Publicerad: (2007) -
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris.
av: Bell, S, et al.
Publicerad: (2006) -
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris.
av: Bell, S, et al.
Publicerad: (2008) -
Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.
av: Peng, Y, et al.
Publicerad: (2007) -
Crystal structure of a ferredoxin reductase for the CYP199A2 system from Rhodopseudomonas palustris.
av: Xu, F, et al.
Publicerad: (2009)