title: Haem-oxygen reactive intermediates: catalysis by the two-step.
abstract: The catalytic schemes of a variety of haem enzymes, including the P450 mono-oxygenases, consist of a number of common reactive haem-oxygen adducts. The characterization of these intermediates by optical and EPR spectroscopies has reinforced the similarity of these intermediate states in a number of haem enzyme systems. Furthermore, the reactivity of these states in P450 and horseradish peroxidase, in which multiple potent oxidants are formed, provides a paradigm for many other haem enzymes.
authors.affiliation: The Center for Biophysics and Computational Biology, University of Illinois Urbana-Champaign, 505 S. Goodwin Avenue, Urbana, IL 61801, USA.
authors.forename: T M
authors.initials: TM
authors.lastname: Makris
authors.forename: I G
authors.initials: IG
authors.lastname: Denisov
authors.forename: S G
authors.initials: SG
authors.lastname: Sligar
mesh_terms: D002384:Catalysis; D006418:Heme / Q000378:metabolism*; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D010100:Oxygen / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013255:Steroid 21-Hydroxylase / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D006418:Heme; D013255:Steroid 21-Hydroxylase; D010100:Oxygen