5JTD

Crystal structure of the Ru(bpy)2PhenA functionalized P450 BM3 L407C heme domain mutant in complex with DMSO.

Summary for 5JTD

• Entry DOI: 10.2210/pdb5jtd/pdb
• Descriptor: Bifunctional cytochrome P450/NADPH--P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, DIMETHYL SULFOXIDE, ... (5 entities in total)
• Functional Keywords: hybrid p450 bm3 enzymes, electron transfer, photosensitizer, photocatalytic activity, oxidoreductase
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm : P14779
• Total number of polymer chains: 2
• Total formula weight: 110468.81

Authors

Kloos, M. (deposition date: 2016-05-09, release date: 2016-10-12, Last modification date: 2024-10-16)

Primary citation

Spradlin, J.,Lee, D.,Mahadevan, S.,Mahomed, M.,Tang, L.,Lam, Q.,Colbert, A.,Shafaat, O.S.,Goodin, D.,Kloos, M.,Kato, M.,Cheruzel, L.E.
Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.
Biochim.Biophys.Acta, 1864:1732-1738, 2016

PubMed Abstract: In order to perform selective CH functionalization upon visible light irradiation, Ru(II)-diimine functionalized P450 heme enzymes have been developed. The sL407C-1 enzyme containing the Ru(bpy)PhenA (bpy=2,2'-bipyridine and PhenA=5-acetamido-1,10-phenanthroline) photosensitizer (1) covalently attached to the non-native single cysteine L407C of the P450BM3 heme domain mutant, displays high photocatalytic activity in the selective CH bond hydroxylation of several substrates.

PubMed: 27639964
DOI: 10.1016/j.bbapap.2016.09.005

Experimental method

X-RAY DIFFRACTION (1.5 Å)