Structural biology of heme monooxygenases.
Over the past few years the number of crystal structures available for heme monooxygenases has substantially increased. Those most closely related to one another are cytochrome P450, nitric oxide synthase, and heme oxygenase. The present mini-review provides a summary of some recently published work on how crystallography and solution studies have provided new insights on function and especially the oxygen activation process. It now appears that in all three monooxygenases highly ordered solvent in the active site serves as direct proton donors to the iron-linked dioxygen; a requirement for splitting the O-O bond. This is in sharp contrast to the related peroxidase family of enzymes where strategically positioned amino acid side chains serve the function of shuttling protons. The P450cam-oxy-complex as well as various mutants in a complex with either oxygen or carbon monoxide have enabled a fairly detailed picture to be developed on the role of specific amino acids and conformational changes in both electron transfer and oxygen activation.
Poulos
Thomas L
TL
Department of Molecular Biology, The Center in Chemical and Structural Biology, University of California, Irvine, Irvine, CA 92697-3900, USA. poulos@uci.edu
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D019001:Nitric Oxide Synthase / Q000737:chemistry* / Q000378:metabolism
D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D019001:Nitric Oxide Synthase; D006419:Heme Oxygenase (Decyclizing)