Pure Appl. Chem., 2004, Vol. 76, No. 2, pp. 335-350
doi:10.1351/pac200476020335
Probing fundamental mechanisms of nitric oxide reactions with metal centers*
P. C. Ford
Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, CA 93106-9510, USA
Abstract:
Studies in this laboratory have been concerned with mapping the chemical properties and mechanisms of NO interactions with hemes and other metal centers. These are models relevant to the mammalian biology of nitric oxide, an important bioregulatory molecule. Presented here will be an overview of flash photolysis kinetics investigations of ferri- and ferro-heme nitrosyl formation in model complexes and several heme proteins. Also described will be ongoing studies of reductive nitrosylation mechanisms involving the reactions of NO with water-soluble Fe(III) porphyrins and ferri-heme proteins and of several Cu(II) model complexes.