Studies of P450 Reaction Intermediates

Structural resolution of oxy-ferrous P450 reveals important differences from the ferrous 

The differential solvation of the active site in the Asn251 and Ala252 mutants is also observed in resonance Raman spectra of the ferric cyanide adducts. Specifically, while the wild-type enz5ane shows exclusive sensitivity to isotopic exchange in the bent conformer, those of the 

Further differences between studies performed on frozen solutions and crystals can be attributable to crystal contacts that may have a crucial impact on the dynamics of the system, thereby changing relative rates of subsequent reaction steps. For example, the lack of accumulation of 

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 

---