Local charge distributions, electric dipole moments, and local electric fields influence reactivity patterns and guide regioselectivities in α-ketoglutarate-dependent non …
Conspectus Non-heme iron dioxygenases catalyze vital processes for human health related
to the biosynthesis of essential products and the biodegradation of toxic metabolites. Often …
to the biosynthesis of essential products and the biodegradation of toxic metabolites. Often …
Second‐coordination sphere effects on selectivity and specificity of heme and nonheme iron enzymes
SP de Visser - Chemistry–A European Journal, 2020 - Wiley Online Library
Mononuclear iron‐containing enzymes are highly versatile oxidants that often react
stereospecifically and/or regioselectively with substrates. Combined experimental and …
stereospecifically and/or regioselectively with substrates. Combined experimental and …
Substrate oxidation by cytochrome P450 enzymes
PR Ortiz de Montellano - Cytochrome P450: structure, mechanism, and …, 2015 - Springer
Cytochrome P450 enzymes catalyze a broad diversity of reactions, including well-
established transformations such as carbon and nitrogen hydroxylation, heteroatom …
established transformations such as carbon and nitrogen hydroxylation, heteroatom …
Significantly shorter Fe–S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase
Abstract Cytochrome P450 (P450) and chloroperoxidase (CPO) are thiolate-ligated haem
proteins that catalyse the activation of carbon hydrogen bonds. The principal intermediate in …
proteins that catalyse the activation of carbon hydrogen bonds. The principal intermediate in …
Hydrogen‐Bonding Interactions Trigger a Spin‐Flip in Iron (III) Porphyrin Complexes
A key step in cytochrome P450 catalysis includes the spin‐state crossing from low spin to
high spin upon substrate binding and subsequent reduction of the heme. Clearly, a weak …
high spin upon substrate binding and subsequent reduction of the heme. Clearly, a weak …
Spectroscopic studies of the cytochrome P450 reaction mechanisms
PJ Mak, IG Denisov - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2018 - Elsevier
The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often
under physiological conditions, catalyze many distinct oxidative transformations on a wide …
under physiological conditions, catalyze many distinct oxidative transformations on a wide …
Functional divergence of heme-thiolate proteins: a classification based on spectroscopic attributes
1. INTRODUCTION Heme proteins are among the most versatile players in the biological
milieu; their functions range widely and include electron transfer, catalysis, and small …
milieu; their functions range widely and include electron transfer, catalysis, and small …
Driving Force for Oxygen Atom Transfer by Heme-Thiolate Enzymes
X Wang, X Wang - A Novel Heme-Thiolate Peroxygenase AaeAPO and Its …, 2016 - Springer
The heme-thiolate peroxygenase Aae APO from Agrocybe aegerita is an important
biocatalyst and P450 analog. We have found that Aae APO compound I can be formed via …
biocatalyst and P450 analog. We have found that Aae APO compound I can be formed via …
Enhanced Reactivities of Iron (IV)‐Oxo Porphyrin Species in Oxidation Reactions Promoted by Intramolecular Hydrogen‐Bonding
High‐valent iron‐oxo species are one of the common intermediates in both biological and
biomimetic catalytic oxidation reactions. Recently, hydrogen‐bonding (H‐bonding) has been …
biomimetic catalytic oxidation reactions. Recently, hydrogen‐bonding (H‐bonding) has been …
Role of the proximal cysteine hydrogen bonding interaction in cytochrome P450 2B4 studied by cryoreduction, electron paramagnetic resonance, and electron …
R Davydov, S Im, M Shanmugam, WA Gunderson… - Biochemistry, 2016 - ACS Publications
Crystallographic studies have shown that the F429H mutation of cytochrome P450 2B4
introduces an H-bond between His429 and the proximal thiolate ligand, Cys436, without …
introduces an H-bond between His429 and the proximal thiolate ligand, Cys436, without …