A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans
dc.contributor.author | Bell, S. | |
dc.contributor.author | Dale, A. | |
dc.contributor.author | Rees, N. | |
dc.contributor.author | Wong, L. | |
dc.date.issued | 2010 | |
dc.description.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 beta-ionone to predominantly 3-R-hydroxy-beta-ionone and 4-hydroxy-beta-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 microM (gram of cell dry weight)(-1) min(-1). These efficient biocatalytic systems have potential uses in preparative scale whole-cell biotransformations. | |
dc.description.statementofresponsibility | Stephen G. Bell, Alison Dale, Nicholas H. Rees, Luet-Lok Wong | |
dc.identifier.citation | Applied Microbiology and Biotechnology, 2010; 86(1):163-175 | |
dc.identifier.doi | 10.1007/s00253-009-2234-y | |
dc.identifier.issn | 0175-7598 | |
dc.identifier.issn | 1432-0614 | |
dc.identifier.orcid | Bell, S. [0000-0002-7457-9727] | |
dc.identifier.uri | http://hdl.handle.net/2440/75177 | |
dc.language.iso | en | |
dc.publisher | Springer-Verlag | |
dc.rights | © Springer-Verlag 2009 | |
dc.source.uri | https://doi.org/10.1007/s00253-009-2234-y | |
dc.subject | Cytochrome P450 | |
dc.subject | Novosphingobium aromaticivorans | |
dc.subject | Electron transfer | |
dc.subject | Ferredoxin reductase | |
dc.subject | Whole-cell biotransformations | |
dc.title | A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans | |
dc.type | Journal article | |
pubs.publication-status | Published |