4H23

Cytochrome P411BM3-CIS cyclopropanation catalyst

Summary for 4H23

• Entry DOI: 10.2210/pdb4h23/pdb
• Related: 4H24
• Descriptor: Cytochrome P450-BM3 variant P411BM3-Cis, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: cytochrome p450, enzymatic cyclopropanation, directed evolution, non-natural function, oxidoreductase
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 2
• Total formula weight: 108677.49

Authors

Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M. (deposition date: 2012-09-11, release date: 2013-06-26, Last modification date: 2023-09-20)

Primary citation

Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M.
A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.
Nat.Chem.Biol., 9:485-487, 2013

PubMed Abstract: Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450(BM3) gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state Fe(III)-to-Fe(II) reduction potential and substantially improves NAD(P)H-driven activity.

PubMed: 23792734
DOI: 10.1038/nchembio.1278

Experimental method

X-RAY DIFFRACTION (3.3 Å)