| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1925809 | Archives of Biochemistry and Biophysics | 2011 | 8 Pages |
Abstract
This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.
Research highlights► EPR/ENDOR spectroscopy of radiolytically cryoreduced oxyheme monooxygenases has identified the active oxidizing species in: (1) cytochrome P450 reactions; (2) the two stages by which NOS generates NO; (3) meso-heme hydroxylation by heme oxygenases. ► It has also demonstrated the influence of substrate in modulating monooxygenase activity.
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Authors
Roman Davydov, Brian M. Hoffman,