Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
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60 YEARS OF POMC: From POMC and α-MSH to PAM, molecular oxygen, copper, and vitamin CAmidation of Bioactive Peptides: The Structure of the Lyase Domain of the Amidating EnzymeCrystal Structure of the Membrane Fusion Protein CusB from Escherichia coliDifferential Reactivity between Two Copper Sites in Peptidylglycine α-Hydroxylating MonooxygenaseCoordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): structural and computational studyThe crystal structure of human dopamine β-hydroxylase at 2.9 Å resolutionEvidence for substrate preorganization in the peptidylglycine α-amidating monooxygenase reaction describing the contribution of ground state structure to hydrogen tunnelingSupplying copper to the cuproenzyme peptidylglycine alpha-amidating monooxygenaseIntermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processingCopper active sites in biologyImino-oxy acetic acid dealkylation as evidence for an inner-sphere alcohol intermediate in the reaction catalyzed by peptidylglycine alpha-hydroxylating monooxygenase.Emerging Evidence on Neutrophil Motility Supporting Its Usefulness to Define Vitamin C Intake Requirements.The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: an X-ray absorption study.The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural roleOxygen Binding, Activation, and Reduction to Water by Copper Proteins.Copper dioxygen (bio)inorganic chemistryThe copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation.Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.X-ray absorption edge spectroscopy and computational studies on LCuO2 species: Superoxide-Cu(II) versus peroxide-Cu(III) bonding.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 MonooxygenaseStopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase.Effects of thioether substituents on the O2 reactivity of beta-diketiminate-Cu(I) complexes: probing the role of the methionine ligand in copper monooxygenasesPeptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function.HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch.Substituted hippurates and hippurate analogs as substrates and inhibitors of peptidylglycine alpha-hydroxylating monooxygenase (PHM).O2 activation by binuclear Cu sites: noncoupled versus exchange coupled reaction mechanismsInterdomain long-range electron transfer becomes rate-limiting in the Y216A variant of tyramine β-monooxygenase.The power of integrating kinetic isotope effects into the formalism of the Michaelis-Menten equation.Carbon monoxide transport and actions in blood and tissues.Vitamin C: the known and the unknown and Goldilocks.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.Inactivation of peptidylglycine α-hydroxylating monooxygenase by cinnamic acid analogs.Inactivation of Met471Cys tyramine β-monooxygenase results from site-specific cysteic acid formation.Reaction mechanism of the bicopper enzyme peptidylglycine α-hydroxylating monooxygenaseTrafficking of a secretory granule membrane protein is sensitive to copper.A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase.Plausible molecular mechanism for activation by fumarate and electron transfer of the dopamine beta-mono-oxygenase reactionEvidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species.Protein Stability and Unfolding Following Glycine Radical Formation.
P2860
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P2860
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@ast
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@en
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@nl
type
label
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@ast
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@en
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@nl
prefLabel
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@ast
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@en
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@nl
P2093
P3181
P356
P1476
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase
@en
P2093
P304
P3181
P356
10.1038/13351
P577
1999-10-01T00:00:00Z