title: The diagnostic substrate bicyclohexane reveals a radical mechanism for bacterial cytochrome P450 in whole cells.
authors.affiliation: Department of Chemistry, Bates College, Lewiston, ME 04240, USA. raustin@bates.edu
authors.forename: Rachel N
authors.initials: RN
authors.lastname: Austin
authors.forename: Dayi
authors.initials: D
authors.lastname: Deng
authors.forename: Yongying
authors.initials: Y
authors.lastname: Jiang
authors.forename: Kate
authors.initials: K
authors.lastname: Luddy
authors.forename: Jan B
authors.initials: JB
authors.lastname: van Beilen
authors.forename: Paul R
authors.initials: PR
authors.lastname: Ortiz de Montellano
authors.forename: John T
authors.initials: JT
authors.lastname: Groves
mesh_terms: D000150:Acinetobacter / Q000201:enzymology*; D001643:Bridged Bicyclo Compounds / Q000737:chemistry / Q000378:metabolism*; D002474:Cell-Free System; D003521:Cyclopropanes / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D015394:Molecular Structure; D009161:Mycobacterium / Q000201:enzymology*; D016958:Pseudomonas putida / Q000378:metabolism
chemical_list: D001643:Bridged Bicyclo Compounds; D003521:Cyclopropanes; C046059:bicyclo(3.1.0)hexane; D003577:Cytochrome P-450 Enzyme System