Cyclic amine functionalisation by engineered cytochrome P450BM3 by Li, Y

“…Cytochrome P450_BM3 from Bacillus megaterium has been extensively engineered to develop biocatalytic pathways to bioactive compounds due to its self-sufficiency, high expression level and promiscuity in substrate recognition. …”

Redox properties of cytochrome p450BM3 measured by direct methods. by Fleming, B, Tian, Y, Bell, S, Wong, L, Urlacher, V, Hill, H

“…Cytochrome p450BM3 is a self-sufficient fatty acid monooxygenase consisting of a diflavin (FAD/FMN) reductase domain and a heme domain fused together in a single polypeptide chain. …”

A P450BM3 toolkit For C-H activation synthesis by Ren, X

“…Since there is widespread interest in the selective functionalisation of C–H bonds, P450s have been extensively studied and evolved, particularly P450_BM3 from <em>Bacillus megaterium</em>, which is catalytically self-sufficient. In this thesis, a P450_BM3 variant library has been developed based on four 'generic accelerators', which have showed enhanced activity towards a broad range of non-natural substrates such as polyaromatic hydrocarbons and terpenes. …”

Enantioselective remote functionalisation of cyclic amines by engineered P450BM3 variants by Zhang, Y

“…This makes P450_BM3 catalytically self-sufficient and promotes high turnover rates. Functionalised cyclic amines are versatile intermediates in drug synthesis and important fragment molecules in drug discovery. …”

Partial fusion of a cytochrome P450 system by carboxy-terminal attachment of putidaredoxin reductase to P450cam (CYP101A1) by Johnson, E, Wong, L

“…Application development of class I CYPs is hampered by their dependence on two redox partners (a ferredoxin and ferredoxin reductase), slowing catalysis compared to self-sufficient CYPs such as CYP102A1 (P450BM3). Previous attempts to address this have fused all three components in several permutations and geometries, with much reduced activity compared to the native system. …”

Engineering terpenoid oxidation by cytochrome P450BM3 for fine chemical synthesis by Chen, W

“…The intramolecular electron transfer process makes P450BM3 catalytically self-sufficient and promotes high turnover rates. P450 enzymes activate C−H bonds via the insertion of an oxygen atom from atmospheric dioxygen and play key roles in the biosynthesis of endogenous compounds (terpenes, alkaloids and steroids).…”

Hydrogen-driven hydrocarbon oxidation by cytochrome P450 enzymes by Urata, K

“…<p>P450_BM3 (CYP102A1) from <em>Bacillus megaterium</em> is a 119 kDa, 1,046-residue polypeptide with the FAD/FMN reductase domain fused to the C-terminus of the haem domain and, as such it is catalytically self-sufficient; only NADPH and oxygen are required for monooxygenase activity. …”

Sesquiterpene oxidation by evolved CYP102A1 (P450BM3) monooxygenase by Cao, Y

“…CYP102A1, also known as P450_BM3 as the 3^rd P450 enzyme identified from <em>Bacillus megaterium</em>, was the first discovered self-sufficient P450 which has been extensively studied as a biocatalyst for decades. …”