Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactionsIron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shiftsUse of ferrous iron by metallo-β-lactamasesOvercoming differences: The catalytic mechanism of metallo-β-lactamasesSpectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzymeMotion of the zinc ions in catalysis by a dizinc metallo-beta-lactamaseProbing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysisInvestigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor bindingStructure and mechanism of copper- and nickel-substituted analogues of metallo-beta-lactamase L1Catalytic role of the metal ion in the metallo-beta-lactamase GOB.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralisProperties and distribution of a metallo-β-lactamase (ALI-1) from the fish pathogen Aliivibrio salmonicida LFI1238.Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.A DNA nanoribbon as a potent inhibitor of metallo-β-lactamases.
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P2860
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 03 October 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
@en
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
@nl
type
label
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
@en
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
@nl
prefLabel
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
@en
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
@nl
P2093
P2860
P356
P1476
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1
@en
P2093
Brian Bennett
Gopalraj Periyannan
Michael W Crowder
Zhenxin Hu
P2860
P304
14207-14216
P356
10.1021/JA8035916
P407
P577
2008-10-03T00:00:00Z