Reactions of water soluble iron(II) and cobalt(II) porphyrins with nitric oxide. Implications for the reactivity of NO and biologically relevant metal centers

1999 ◽  
pp. 1843 ◽  
Author(s):  
Leroy E. Laverman ◽  
Peter C. Ford
1997 ◽  
Vol 119 (51) ◽  
pp. 12663-12664 ◽  
Author(s):  
Leroy E. Laverman ◽  
Mikio Hoshino ◽  
Peter C. Ford

2003 ◽  
Vol 349 ◽  
pp. 17-22 ◽  
Author(s):  
Shigeo Nakagawa ◽  
Tetsuya Yashiro ◽  
Hiroki Munakata ◽  
Hiroyasu Imai ◽  
Yoshio Uemori

2004 ◽  
Vol 76 (2) ◽  
pp. 335-350 ◽  
Author(s):  
P. C. Ford

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.


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