A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡ - Wikidata - awgldk - TriplyDB

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

http://www.wikidata.org/entity/Q27652469

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X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters Cysteine Dioxygenase Structures from pH4 to 9: Consistent Cys-Persulfenate Formation at Intermediate pH and a Cys-Bound Enzyme at Higher pH Linking Crystallographic Model and Data Quality Thiol dioxygenases: unique families of cupin proteins.Better models by discarding data?Sulfur versus iron oxidation in an iron-thiolate model complex Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications.Divergence and convergence in enzyme evolution.Spectroscopic and computational investigation of iron(III) cysteine dioxygenase: implications for the nature of the putative superoxo-Fe(III) intermediate.Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes.Spectroscopic and Computational Investigation of the H155A Variant of Cysteine Dioxygenase: Geometric and Electronic Consequences of a Third-Sphere Amino Acid Substitution The "Gln-Type" Thiol Dioxygenase from Azotobacter vinelandii is a 3-Mercaptopropionic Acid Dioxygenase.Spectroscopic and computational characterization of the NO adduct of substrate-bound Fe(II) cysteine dioxygenase: insights into the mechanism of O2 activation.Computational modelling of oxygenation processes in enzymes and biomimetic model complexes.A jack-of-all-trades: 2-mercaptosuccinic acid.Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.O2 activation by bis(imino)pyridine iron(II)-thiolate complexes.Iron(II)-thiolate S-oxygenation by O2: synthetic models of cysteine dioxygenase.Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs.Metal-Assisted Oxo Atom Addition to an Fe(III) Thiolate.Preparation of non-heme {FeNO}7 models of cysteine dioxygenase: sulfur versus nitrogen ligation and photorelease of nitric oxide.Structure-Based Insights into the Role of the Cys-Tyr Crosslink and Inhibitor Recognition by Mammalian Cysteine Dioxygenase Addition of dioxygen to an N4S(thiolate) iron(II) cysteine dioxygenase model gives a structurally characterized sulfinato-iron(II) complex Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers.Mercaptosuccinate dioxygenase, a cysteine dioxygenase homologue, from Variovorax paradoxus strain B4 is the key enzyme of mercaptosuccinate degradation.Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O2-dependent oxidation of primary alcohols.Structure and mechanism leading to formation of the cysteine sulfinate product complex of a biomimetic cysteine dioxygenase model.A trispyrazolylborato iron cysteinato complex as a functional model for the cysteine dioxygenase.Ein Trispyrazolylborato-Eisen-Cysteinato-Komplex als funktionelles Modell für die Cystein-Dioxygenase

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P2860

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

http://www.wikidata.org/entity/Q27652469

description

2008 nî lūn-bûn

@nan

2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@ast

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@en

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@nl

type

label

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@ast

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@en

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@nl

prefLabel

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@ast

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@en

A Putative Fe 2+ -Bound Persulfenate Intermediate in Cysteine Dioxygenase † ‡

@nl

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A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase

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P2093

Chad R Simmons

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David J Schuller

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John E Dominy

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Kalyanaraman Krishnamoorthy

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Martha H Stipanuk

http://www.w3.org/2001/XMLSchema#string

Spencer L Granett

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Tadhg P Begley

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P2860

Structure and mechanism of mouse cysteine dioxygenase

Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron

Crystal Structures of Fe2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates

Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation

Probes of the catalytic site of cysteine dioxygenase

Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine.

Non-heme iron-dependent dioxygenases: unravelling catalytic mechanisms for complex enzymatic oxidations.

The redox regulation of thiol dependent signaling pathways in cancer.

Cysteine dioxygenase: structure and mechanism.

Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity.

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10.1021/BI801546N

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18847220

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