Ferrous-dioxygen

Denisov, I.G., Grinkova, Y.V., Baas, B.J. and Sligar, S.G. (2006) The ferrous-dioxygen intermediate in human cytochrome P450 3 A4. Substrate dependence of formation and decay kinetics. Journal of Biological Chemistry, 281 (33), 23313-23318. 

Estabrook, R.W., Hildebrandt, A.G., Baron, J., Netter, K.J. and Leibman, K. (1971) A new spectral intermediate associated with cytochrome P-450 function in liver microsomes. Biochemical and Biophysical Research Communications, 42 (1), 132-139. Pompon, D. and Coon, M.J. (1984) On the mechanism of action of cytochrome P-450. Oxidation and reduction of the ferrous dioxygen complex of liver microsomal cytochrome P-450 by cytochrome b5. Journal of Biological Chemistry, 259 (24), 15377-15385. Hildebrandt, A. and Estabrook, R.W. (1971) Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions. Archives of Biochemistry and Biophysics, 143 (1), 66-79. 

Harris, D., Loew, G.H., and Waskell, L. (1998) Structure and spectra of ferrous dioxygen and reduced ferrous dioxygen model cytochrome P450, J. Am. Chem. Soc. 120, 4308-4318. 

It is noteworthy that Aust and coworkers have shown that in vitro lipid peroxidation initiated by ferrous-ADP or ferrous-AMP complexes was strongly stimulated by the presence of the analogous ferric complexes, with no effect of either SOD, catalase or OH scavengers [156,157]. This suggests that a ferrous-dioxygen-ferric chelate may serve as a potent free radical initiator of its own. 

Ferrous porphyrin is a good dioxygen binder, and this leads to the binding of molecular oxygen to produce the LS ferrous-dioxygen complex,... 

In order to resolve structural components potentially involved in proton donation to a reduced ferrous-dioxygen or peroxo-anion species. 

Given the dynamic nature of both intermediates and the isomerization of amino acids of side chains occurring during catalysis, it is not surprising that a number of computational studies have provided subtly different structural mechanisms for the acid-alcohol pair in P450 catalysis. Molecular dynamics simulations of the ferrous-dioxygen... 

Oxidation of nitric oxide by ferrous-dioxygen adducts of hemoproteins occurs accidentally in blood (with hemoglobin) but also as physiological function for certain bacterial globins (e.g., fiavohemoglobin) the mechanism of this reaction appears to entail ferric-peroxynitrite adducts at the heme, whose extremely short lifetimes were predicted by DFT calculations [50, 51]. 

Pompon D, Coon MJ (1984) On the mechanism of action of cytochrome P-450. Oxidation and reduction of the ferrous dioxygen complex of liver microsomal cytochrome P-450 by cytochrome bj. J Biol Chem 259 15377-15385... 

Oxygen Binding and the Structure of the Ferrous Dioxygen Complex... 

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