Oxygen-binding hemoproteins

Jameson, G. B., Molinaro, F. S., Ibers, etal., Models for the active-site of oxygen-binding hemoproteins - dioxygen binding-properties and the structures of (2-methylimidazole)-meso-tetra (a,a,a,a-ortho-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct. J. Am. Chem. Soc. 1980, 102, 3224-3237. 

Collman JP et al (1975) Picket fence porphyrins . Synthetic models for oxygen binding hemoproteins. J Am Chem Soc 97 1427-1439... 

The oxygen-binding hemoproteins myoglobin and hemoglobin have been most thoroughly investigated with regard to their three-dimensional... 

Cytochrome P-450 enzymes have been isolated from a variety of mammalian tissues, insects, plants, yeasts and bacteria. The P-450 cytochromes (Gunter and Turner, 1991) are membrane bound mono-oxygenase enzymes which catalyse oxygen atom transfer to entrapped non-polar substrates. The binding of carbon monoxide to the enzyme produces a split in the 420 nm Soret band to give bands at 364 and 450 nm. The absorption at 450 nm distinguishes the hemoprotein from all others and hence provides... 

NADPH-cytochrome P-450 reductase, a flavoprotein that transfers electrons from NADH to cytochrome P-450, reducing the iron of the P-450 hemoprotein from the Fe(III) to the Fe(II) state so that molecular oxygen will bind to it in the first stages of its action and... 

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