Designed whole-cell-catalysis-assisted synthesis of 9,11-secosterols

• Marek Kõllo,
• Marje Kasari,
• Villu Kasari,
• Tõnis Pehk,
• Ivar Järving,
• Margus Lopp,
• Arvi Jõers and
• Tõnis Kanger

Beilstein J. Org. Chem. 2021, 17, 581–588, doi:10.3762/bjoc.17.52

• the chemical oxidative cleavage of the 9,11-C–C bond. For the hydroxylation, we used a biocatalyst derived from an Escherichia coli laboratory strain BL21 (DE3) overexpressing the kshA5 and kshB genes from Rhodococcus. rhodochrous. Cortisol (1) was chosen as a model steroidal structure. Results and

Regio- and stereoselective oxidation of unactivated C–H bonds with Rhodococcus rhodochrous

• Elaine O’Reilly,
• Suzanne J. Aitken,
• Gideon Grogan,
• Paul P. Kelly,
• Nicholas J. Turner and
• Sabine L. Flitsch

Beilstein J. Org. Chem. 2012, 8, 496–500, doi:10.3762/bjoc.8.56

• Chemistry, University of York, Heslington, York, YO10 5DD, UK, Tel: +44 (0)1904 328256 10.3762/bjoc.8.56 Abstract The ability of Rhodococcus rhodochrous (NCIMB 9703) to catalyse the regio- and stereoselective hydroxylation of a range of benzyloxy-substituted heterocycles has been investigated. Incubation

• isomers in yields of up to 26%. Most interestingly, 2-(4-nitrobenzyloxy)tetrahydrofuran and 2-(4-nitrobenzyloxy)tetrahydropyran were transformed in high yields to the 4-hydroxylated and 5-hydroxylated products, respectively. Keywords: biocatalysis; cytochrome P450; hydroxylation; Rhodococcus rhodochrous

• dioxygenases has made them the focus of research into bioremediation and biocatalyst development [12]. The soil bacterium Rhodococcus rhodochrous (also referred to as Corynebacterium sp. 7E1C, Rhodococcus rhodochrous ATCC 19067 and Gordonia rubripertinctus 7E1C) is known to oxidise a wide variety of aliphatic