Differential Reactivity between Two Copper Sites in Peptidylglycine α-Hydroxylating Monooxygenase - Wikidata - wikimedia - TriplyDB

Differential Reactivity between Two Copper Sites in Peptidylglycine α-Hydroxylating Monooxygenase

Differential Reactivity between Two Copper Sites in Peptidylglycine α-Hydroxylating Monooxygenase

http://www.wikidata.org/entity/Q27665185

about

Protein design: toward functional metalloenzymes Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational study Copper active sites in biology Artificial metalloenzymes derived from three-helix bundles Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase Nitrite Reductase Activity in Engineered Azurin Variants HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch.Computational study of the activated O(H) state in the catalytic mechanism of cytochrome c oxidase.De novo-designed metallopeptides with type 2 copper centers: modulation of reduction potentials and nitrite reductase activities.Binding of copper and silver to single-site variants of peptidylglycine monooxygenase reveals the structure and chemistry of the individual metal centers.Substrate-Induced Carbon Monoxide Reactivity Suggests Multiple Enzyme Conformations at the Catalytic Copper M-Center of Peptidylglycine Monooxygenase.A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase.Copper(I)-Dioxygen Adducts and Copper Enzyme Mechanisms.Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.Structure-oriented bioinformatic approach exploring histidine-rich clusters in proteins.Copper coordinated ligand thioether-S and NO2(-) oxidation: relevance to the CuM site of hydroxylases.Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go

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Differential Reactivity between Two Copper Sites in Peptidylglycine α-Hydroxylating Monooxygenase

http://www.wikidata.org/entity/Q27665185

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

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name

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@ast

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@en

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@nl

type

label

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@ast

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

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Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

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prefLabel

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@ast

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@en

Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

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Journal of the American Chemical Society

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Differential Reactivity betwee ...... α-Hydroxylating Monooxygenase

@en

P2093

Betty A Eipper

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Eduardo E Chufán

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

Richard E Mains

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Xavier Siebert

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P2860

Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase

Crystal structure of a novel red copper protein from Nitrosomonas europaea

Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine

pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase

Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase

The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis † , ‡

High resolution crystal structure of Rubrivivax gelatinosus cytochrome c'

Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules

Amidation of Bioactive Peptides: The Structure of the Lyase Domain of the Amidating Enzyme

Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications

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15565-72

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scholarly article

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10.1021/JA103117R

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44

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132

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20958070

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