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

scholarly journals Cytochrome P450 Alkane Hydroxylases of the CYP153 Family Are Common in Alkane-Degrading Eubacteria Lacking Integral Membrane Alkane Hydroxylases

2006 ◽  
Vol 72 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Jan B. van Beilen ◽  
Enrico G. Funhoff ◽  
Alexander van Loon ◽  
Andrea Just ◽  
Leo Kaysser ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Pseudomonas Putida ◽  
Chain Length ◽  
Nonheme Iron ◽  
Cytochrome P450 Enzymes ◽  
Medium Chain ◽  
Ferredoxin Reductase ◽  
Medium Chain Length ◽  
Reductase Gene ◽  
Alkane Hydroxylases

ABSTRACT Several strains that grow on medium-chain-length alkanes and catalyze interesting hydroxylation and epoxidation reactions do not possess integral membrane nonheme iron alkane hydroxylases. Using PCR, we show that most of these strains possess enzymes related to CYP153A1 and CYP153A6, cytochrome P450 enzymes that were characterized as alkane hydroxylases. A vector for the polycistronic coexpression of individual CYP153 genes with a ferredoxin gene and a ferredoxin reductase gene was constructed. Seven of the 11 CYP153 genes tested allowed Pseudomonas putida GPo12 recombinants to grow well on alkanes, providing evidence that the newly cloned P450s are indeed alkane hydroxylases.

scholarly journals Reactivity Patterns of (Protonated) Compound II and Compound I of Cytochrome P450: Which is the Better Oxidant?

2017 ◽  
Vol 23 (26) ◽  
pp. 6406-6418 ◽  
Author(s):  
Xiao-Xi Li ◽  
Verònica Postils ◽  
Wei Sun ◽  
Abayomi S. Faponle ◽  
Miquel Solà ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Compound I ◽  
Compound Ii

scholarly journals Catalytic strategy for carbon−carbon bond scission by the cytochrome P450 OleT

2016 ◽  
Vol 113 (36) ◽  
pp. 10049-10054 ◽  
Author(s):  
Job L. Grant ◽  
Megan E. Mitchell ◽  
Thomas Michael Makris
Keyword(s):  
Cytochrome P450 ◽  
Organic Substrates ◽  
Compound I ◽  
Kinetic Isotope ◽  
Carbon Carbon Bond ◽  
Bond Scission ◽  
Decarboxylation Reaction ◽  
Form Compound ◽  
Compound Ii ◽  
Alkene Synthesis

OleT is a cytochrome P450 that catalyzes the hydrogen peroxide-dependent metabolism of Cn chain-length fatty acids to synthesize Cn-1 1-alkenes. The decarboxylation reaction provides a route for the production of drop-in hydrocarbon fuels from a renewable and abundant natural resource. This transformation is highly unusual for a P450, which typically uses an Fe4+−oxo intermediate known as compound I for the insertion of oxygen into organic substrates. OleT, previously shown to form compound I, catalyzes a different reaction. A large substrate kinetic isotope effect (≥8) for OleT compound I decay confirms that, like monooxygenation, alkene formation is initiated by substrate C−H bond abstraction. Rather than finalizing the reaction through rapid oxygen rebound, alkene synthesis proceeds through the formation of a reaction cycle intermediate with kinetics, optical properties, and reactivity indicative of an Fe4+−OH species, compound II. The direct observation of this intermediate, normally fleeting in hydroxylases, provides a rationale for the carbon−carbon scission reaction catalyzed by OleT.

A mononuclear nonheme iron(iv)-oxo complex which is more reactive than cytochrome P450 model compound I

2011 ◽  
Vol 2 (6) ◽  
pp. 1039 ◽  
Author(s):  
Mi Sook Seo ◽  
Nam Hee Kim ◽  
Kyung-Bin Cho ◽  
Jeong Eun So ◽  
Seon Kyung Park ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Model Compound ◽  
Nonheme Iron ◽  
Compound I

scholarly journals X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

2008 ◽  
Vol 105 (24) ◽  
pp. 8179-8184 ◽  
Author(s):  
M. Newcomb ◽  
J. A. Halgrimson ◽  
J. H. Horner ◽  
E. C. Wasinger ◽  
L. X. Chen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Spectroscopic Characterization ◽  
X Ray ◽  
Compound Ii ◽  
X Ray Absorption

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.

Molecular evolution of a cytochrome P450 for the synthesis of potential antidepressant (2R,6R)-hydroxynorketamine

2021 ◽  
Author(s):  
Ansgar Bokel ◽  
Michael C. Hutter ◽  
Vlada B. Urlacher
Keyword(s):  
Cytochrome P450 ◽  
Molecular Evolution ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Effective Synthesis

Engineered cytochrome P450 monooxygenase CYP154E1 enables the effective synthesis of the potential antidepressant (2R,6R)-hydroxynorketamine via N-demethylation and regio- and stereoselective hydroxylation of (R)-ketamine.

Comparison of mechanism-based inhibition of human cytochrome P450 2C19 by ticlopidine, clopidogrel, and prasugrel

Xenobiotica ◽  
2009 ◽  
Vol 00 (00) ◽  
pp. 090901052457079-8
Author(s):  
Y. Nishiya ◽  
K. Hagihara ◽  
A. Kurihara ◽  
N. Okudaira ◽  
N.A. Farid ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Human Cytochrome ◽  
Cytochrome P450 2C19

Deactivation of anti-cancer drug letrozole to a carbinol metabolite by polymorphic cytochrome P450 2A6 in human liver microsomes

Xenobiotica ◽  
2009 ◽  
Vol 00 (00) ◽  
pp. 090901052053001-8
Author(s):  
K. Murai ◽  
H. Yamazaki ◽  
K. Nakagawa ◽  
R. Kawai ◽  
T. Kamataki
Keyword(s):  
Cytochrome P450 ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
Cancer Drug ◽  
Anti Cancer ◽  
Cytochrome P450 2A6
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