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.
*Plenary lecture presented at the 2nd Santa Mar�a Workshop
on Chemistry Devoted to Bioinorganic Chemistry, Santa Mar�a del Mar,
Havana, Cuba, 7-11 July 2003. Other presentations are published in this
issue, pp. 321-388.
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