The mechanism of heme oxygenase.
Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be written for the steps that convert alpha-meso-hydroxyheme to biliverdin, but these mechanisms must be validated before this complex reaction sequence can be fully understood. The salient conclusion appears to be that the heme-oxygenase reaction reflects the absence of interactions that channel the reaction towards a ferryl species, rather than the presence of interactions that specifically promote heme oxidation.
Montellano
P R
PR
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, 94143-0446, USA. ortiz@cgl.ucsf.edu
D000818:Animals; D001664:Biliverdine / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry* / Q000378:metabolism*; D051547:Heme Oxygenase-1; D006801:Humans; D006900:Hydroxylation; D008565:Membrane Proteins; D008956:Models, Chemical
D008565:Membrane Proteins; D006418:Heme; C496541:HMOX1 protein, human; D006419:Heme Oxygenase (Decyclizing); D051547:Heme Oxygenase-1; D001664:Biliverdine