Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies. Academic Article

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.

authors

• Musser, Siegfried

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Davydov, R., & Hoffman, B. M

citation count

• 45

complete list of authors

• Davydov, Roman||Hoffman, Brian M

publication date

• March 2011

publisher

• Elsevier BV  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Animals
• Cytochrome P-450 Enzyme System
• Electron Spin Resonance Spectroscopy
• Enzyme Activation
• Heme Oxygenase (decyclizing)
• Humans
• Models, Molecular
• Nitric Oxide Synthase

PubMed Central ID

• 20854788

Digital Object Identifier (DOI)

• 10.1016/j.abb.2010.09.013

start page

• 36

end page

• 43

volume

• 507

issue

• 1