Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris.
CYP199A2 from Rhodopseudomonas palustris CGA009 is a heme monooxygenase that catalyzes the oxidation of para-substituted benzoic acids. CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin (Pux) and a flavoprotein p...
Main Authors: | Bell, S, Xu, F, Johnson, E, Forward, I, Bartlam, M, Rao, Z, Wong, L |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2010
|
Similar Items
-
Crystal structure of a ferredoxin reductase for the CYP199A2 system from Rhodopseudomonas palustris.
by: Xu, F, et al.
Published: (2009) -
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris.
by: Bell, S, et al.
Published: (2008) -
Crystal structure of a ferredoxin reductase for the CYP199A2 system from Rhodopseudomonas palustris (vol 77, pg 867, 2009)
by: Xu, F, et al.
Published: (2010) -
Selective oxidative demethylation of veratric acid to vanillic acid by CYP199A4 from Rhodopseudomonas palustris HaA2.
by: Bell, S, et al.
Published: (2010) -
Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.
by: Peng, Y, et al.
Published: (2007)