scholarly journals Characterization and reactivity study of non-heme high-valent iron–hydroxo complexes

2021 ◽  
Author(s):  
Kritika Keshari ◽  
Moumita Bera ◽  
Lucía Velasco ◽  
Sandip Munshi ◽  
Geetika Gupta ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Radical Complex ◽  
Hydroxo Complexes ◽  
Reactivity Study ◽  
High Valent ◽  
Compound Ii

One-electron oxidation of an FeIII–OH complex (1) results in the formation of a FeIII–OH ligand radical complex (2). Its reaction with (C6H5)3C˙ results in the formation of (C6H5)3COH, which is a functional mimic of compound II of cytochrome P450.

Resonance Raman Study of a High-valent Fe=O Porphyrin Complex as a Model for Peroxidase Compound II

2010 ◽  
Vol 39 (4) ◽  
pp. 332-333 ◽  
Author(s):  
Hirohito Ishimaru ◽  
Hiroshi Fujii ◽  
Takashi Ogura
Keyword(s):  
Resonance Raman ◽  
Porphyrin Complex ◽  
Raman Study ◽  
High Valent ◽  
Compound Ii

The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection

2008 ◽  
Vol 412 (2) ◽  
pp. 257-264 ◽  
Author(s):  
Hans-Petter Hersleth ◽  
Ya-Wen Hsiao ◽  
Ulf Ryde ◽  
Carl Henrik Görbitz ◽  
K. Kristoffer Andersson
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide ◽  
Data Collection ◽  
Intermediate Compound ◽  
Crystallographic Data ◽  
X Rays ◽  
Biologically Relevant ◽  
Short Annealing ◽  
High Valent ◽  
Compound Ii

Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallographic data collection. We have generated and solved the 1.30 Å (1 Å=0.1 nm) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe–O distance of 1.8 Å and O–O bond of 1.3 Å in accordance with a FeII–O–O− (or FeIII–O–O2−) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metalloproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O–O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction.

scholarly journals A Mononuclear Nonheme Iron(IV)–Amido Complex Relevant for the Compound II Chemistry of Cytochrome P450

2018 ◽  
Vol 141 (1) ◽  
pp. 80-83 ◽  
Author(s):  
Xiaoyan Lu ◽  
Xiao-Xi Li ◽  
Mi Sook Seo ◽  
Yong-Min Lee ◽  
Martin Clémancey ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Nonheme Iron ◽  
Compound Ii

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

2001 ◽  
Vol 40 (15) ◽  
pp. 2874-2878 ◽  
Author(s):  
François Ogliaro ◽  
Samüel P. de Visser ◽  
John T. Groves ◽  
Sason Shaik
Keyword(s):  
Cytochrome P450 ◽  
High Valent

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

2001 ◽  
Vol 113 (15) ◽  
pp. 2958-2962 ◽  
Author(s):  
François Ogliaro ◽  
Samüel P. de Visser ◽  
John T. Groves ◽  
Sason Shaik
Keyword(s):  
Cytochrome P450 ◽  
High Valent

Electrochemical generation of a high-valent state of cytochrome P450

2006 ◽  
Vol 100 (4) ◽  
pp. 519-523 ◽  
Author(s):  
Andrew K. Udit ◽  
Michael G. Hill ◽  
Harry B. Gray
Keyword(s):  
Cytochrome P450 ◽  
Electrochemical Generation ◽  
Valent State ◽  
High Valent
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