Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue

Author(s):  
François Ogliaro ◽  
Samüel P. de Visser ◽  
John T. Groves ◽  
Sason Shaik
Keyword(s):  
2001 ◽  
Vol 113 (15) ◽  
pp. 2958-2962 ◽  
Author(s):  
François Ogliaro ◽  
Samüel P. de Visser ◽  
John T. Groves ◽  
Sason Shaik
Keyword(s):  

2006 ◽  
Vol 100 (4) ◽  
pp. 519-523 ◽  
Author(s):  
Andrew K. Udit ◽  
Michael G. Hill ◽  
Harry B. Gray

2019 ◽  
Vol 23 (04n05) ◽  
pp. 358-366 ◽  
Author(s):  
Huriye Erdogan

The intermediates operating in the cytochrome P450 catalytic cycle have been investigated for more than half a century, fascinating many enzymologists. Each intermediate has its unique role to carry out diverse oxidations. Natural time course of the catalytic cycle is quite fast, hence, not all of the reactive intermediates could be isolated during physiological catalysis. Different high-valent iron intermediates have been proposed as primary oxidants: the candidates are compound 0 (Cpd 0, [FeOOH][Formula: see text]P450) and compound I (Cpd I, Fe(IV)[Formula: see text]O por[Formula: see text]P450). Among them, the role of Cpd I in hydroxylation is fairly well understood due the discovery of the peroxide shunt. This review endeavors to put the outstanding research efforts conducted to isolate and characterize the intermediates together. In addition to spectral features of each intermediate in the catalytic cycle, the oxidizing powers of Cpd 0 and Cpd I will be discussed along with most recent scientific findings.


2001 ◽  
Vol 113 (19) ◽  
pp. 3612-3612 ◽  
Author(s):  
François Ogliaro ◽  
Samüel P. de Visser ◽  
John T. Groves ◽  
Sason Shaik
Keyword(s):  

2005 ◽  
Vol 44 (15) ◽  
pp. 5379-5387 ◽  
Author(s):  
M. Elisa Crestoni ◽  
S. Fornarini

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