Chemical Communications · 1998 · 17 citations · 8 references
Life SciencesBiochemistryChemistryBiocatalysisCatalysisEnzymologyCatalytic MechanismsEnzymatic CatalysisEnzyme DiscoveryEnzyme FunctionEnzyme-substrate RecognitionHydrolase CatalysisEliminationHydrolase DiscoveryHydrolysis Reaction MechanismNickel EnzymesUrea HydrolysisX-ray Crystallography Interpretation
Reactions of glutarodihydroxamic acid with the hydrolase enzyme urease models, [Ni2(µ-H2O)(OAc)4(tmen)2] and [Ni2(OAc)3(urea)(tmen)2][OTf], lead to novel hydroxylamine elimination and formation of [Ni2(OAc)2{µ-O(N)(OC)2(CH2)3}(tmen)2][OTf] and the tetramer [Ni4(OAc)2(gluA2)2(tmen)4][OTf]2, respectively, both of which are structurally characterised by X-ray crystallography.
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The crystal structure of urease from Klebsiella aerogenes
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Hydroxamate-Bridged Dinuclear Nickel Complexes as Models for Urease Inhibition
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