NDLI: A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans

Content Provider	Springer Nature Link
Author	Bell, Stephen G. Dale, Alison Rees, Nicholas H. Wong, Luet Lok
Copyright Year	2009
Abstract	Cytochrome P450 (CYP) enzymes of the CYP101 and CYP111 families from Novosphingobium aromaticivorans are heme monooxygenases that catalyze the hydroxylation of a range of terpenoid compounds. CYP101D1 and CYP101D2 oxidized camphor to 5-exo-hydroxycamphor. CYP101B1 and CYP101C1 oxidized β-ionone to predominantly 3-R-hydroxy-β-ionone and 4-hydroxy-β-ionone, respectively. CYP111A2 oxidized linalool to 8-hydroxylinalool. Physiologically, these CYP enzymes could receive electrons from Arx, a [2Fe-2S] ferredoxin equivalent to putidaredoxin from the CYP101A1 system from Pseudomonas putida. A putative ferredoxin reductase (ArR) in the N. aromaticivorans genome, with high amino acid sequence homology to putidaredoxin reductase, has been over-produced in Escherichia coli and found to support substrate oxidation by these CYP enzymes via Arx with both high activity and coupling of product formation to NADH consumption. The ArR/Arx electron-transport chain has been co-expressed with the CYP enzymes in an E. coli host to provide in vivo whole-cell substrate oxidation systems that could produce up to 6.0 g L−1 of 5-exo-hydroxycamphor at rates of up to 64 μM (gram of cell dry weight)−1 min−1. These efficient biocatalytic systems have potential uses in preparative scale whole-cell biotransformations.
Starting Page	163
Ending Page	175
Page Count	13
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	86
Issue Number	1
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-09-25
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Cytochrome P450 Novosphingobium aromaticivorans Electron transfer Ferredoxin reductase Whole-cell biotransformations Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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