3VM4

Cytochrome P450SP alpha (CYP152B1) in complex with (R)-ibuprophen

Summary for 3VM4

• Entry DOI: 10.2210/pdb3vm4/pdb
• Related: 3AWM
• Descriptor: Fatty acid alpha-hydroxylase, PROTOPORPHYRIN IX CONTAINING FE, (2R)-2-[4-(2-methylpropyl)phenyl]propanoic acid, ... (5 entities in total)
• Functional Keywords: cytochrome p450, oxidoreductase
• Biological source: Sphingomonas paucimobilis
• Total number of polymer chains: 1
• Total formula weight: 46684.96

Authors

Fujishiro, T.,Shoji, O.,Nagano, S.,Sugimoto, H.,Shiro, Y.,Watanabe, Y. (deposition date: 2011-12-08, release date: 2012-05-09, Last modification date: 2023-11-08)

Primary citation

Fujishiro, T.,Shoji, O.,Kawakami, N.,Watanabe, T.,Sugimoto, H.,Shiro, Y.,Watanabe, Y.
Chiral-substrate-assisted stereoselective epoxidation catalyzed by H2O2-dependent cytochrome P450SP alpha
Chem Asian J, 7:2286-2293, 2012

PubMed Abstract: The stereoselective epoxidation of styrene was catalyzed by H(2) O(2) -dependent cytochrome P450(SPα) in the presence of carboxylic acids as decoy molecules. The stereoselectivity of styrene oxide could be altered by the nature of the decoy molecules. In particular, the chirality at the α-positions of the decoy molecules induced a clear difference in the chirality of the product: (R)-ibuprofen enhanced the formation of (S)-styrene oxide, whereas (S)-ibuprofen preferentially afforded (R)-styrene oxide. The crystal structure of an (R)-ibuprofen-bound cytochrome P450(SPα) (resolution 1.9 Å) revealed that the carboxylate group of (R)-ibuprofen served as an acid-base catalyst to initiate the epoxidation. A docking simulation of the binding of styrene in the active site of the (R)-ibuprofen-bound form suggested that the orientation of the vinyl group of styrene in the active site agreed with the formation of (S)-styrene oxide.

PubMed: 22700535
DOI: 10.1002/asia.201200250

Experimental method

X-RAY DIFFRACTION (1.94 Å)