Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction. - Wikidata - awgldk - TriplyDB

Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction.

Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction.

http://www.wikidata.org/entity/Q34914775

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Structure and mechanism of mouse cysteine dioxygenase Characterization of Active Site Structure in CYP121: A CYTOCHROME P450 ESSENTIAL FOR VIABILITY OF MYCOBACTERIUM TUBERCULOSIS H37Rv Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3 P450cam Visits an Open Conformation in the Absence of Substrate ,Structural and Biochemical Characterization of Mycobacterium tuberculosis CYP142: EVIDENCE FOR MULTIPLE CHOLESTEROL 27-HYDROXYLASE ACTIVITIES IN A HUMAN PATHOGEN Substrate Preferences and Catalytic Parameters Determined by Structural Characteristics of Sterol 14α-Demethylase (CYP51) from Leishmania infantum Key Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate Bias Human P450-like oxidation of diverse proton pump inhibitor drugs by 'gatekeeper' mutants of flavocytochrome P450 BM3 Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily Redox and chemical activities of the hemes in the sulfur oxidation pathway enzyme SoxAX Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1. Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium.Characterization of heme environment and mechanism of peroxide bond cleavage in human prostacyclin synthase Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-dioxygenase-1 Characterization of the proximal ligand in the P420 form of inducible nitric oxide synthase.Characterization of Cupriavidus metallidurans CYP116B1--a thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein.Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}Biological inorganic chemistry at the beginning of the 21st century.Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing.The role of heme binding by DNA-protective protein from starved cells (Dps) in the Tolerance of Porphyromonas gingivalis to heme toxicity.Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase.Transcriptional regulation of insulin-degrading enzyme modulates mitochondrial amyloid β (Aβ) peptide catabolism and functionality.Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase.Cytochrome P450/redox partner fusion enzymes: biotechnological and toxicological prospects.Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.Formation and characterization of an all-ferrous Rieske cluster and stabilization of the [2Fe-2S]0 core by protonation.Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.The H93G Myoglobin Cavity Mutant as a Versatile Scaffold for Modeling Heme Iron Coordination Structures in Protein Active Sites and Their Characterization with Magnetic Circular Dichroism Spectroscopy.The Mycobacterium tuberculosis cytochromes P450: physiology, biochemistry & molecular intervention.Modulation of nuclear receptor function by cellular redox poise.NPY binds with heme to form a NPY-heme complex: enhancing peroxidase activity in free heme and promoting NPY nitration and inactivation.Metalloprotein and metallo-DNA/RNAzyme design: current approaches, success measures, and future challenges.In vitro oxidative decarboxylation of free fatty acids to terminal alkenes by two new P450 peroxygenases.Investigations of heme ligation and ligand switching in cytochromes p450 and p420.Investigation of the mechanism of formation of a thiolate-ligated Fe(III)-OOH Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11.Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutant Catalytic Determinants of Alkene Production by the Cytochrome P450 Peroxygenase OleTJE.Alkylamine-ligated H93G myoglobin cavity mutant: a model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f.A natural heme-signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω-hydroxylation.Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin: proposed role for tetrahydrobiopterin as a proton donor.

P2860

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P2860

Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction.

http://www.wikidata.org/entity/Q34914775

description

2003 nî lūn-bûn

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2003 թուականի Մարտին հրատարակուած գիտական յօդուած

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2003 թվականի մարտին հրատարակված գիտական հոդված

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2003年の論文

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name

Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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type

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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PNAS.0737142100

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Proceedings of the National Academy of Sciences of the United States of America

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Neutral thiol as a proximal li ...... hiolate ligation on reduction.

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Jeffrey A Sigman

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Masanori Sono

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Roshan Perera

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Thomas D Pfister

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P2860

Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly

A photolysis-triggered heme ligand switch in H93G myoglobin.

Heme-Containing Oxygenases.

H93G myoglobin cavity mutant as versatile template for modeling heme proteins: magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes.

Magnetic circular dichroism of ferrous carbonyl adducts of cytochromes P-450 and P-420 and their synthetic models: further evidence for mercaptide as the fifth ligand to iron.

Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase.

Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.

Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: characterization and their catalytic activities.

Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: evidence for tyrosinate ligation to the ferric enzyme heme iron.

Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide syntha

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10.1073/PNAS.0737142100

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100

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2003-03-24T00:00:00Z

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12655049

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