Oded Kleifeld
Weizmann Institute of Science
9 Papers
163 Citations
Oded Kleifeld is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Active site & Matrix metalloproteinase. The author has an hindex of 8, co-authored 9 publications.
Chat about Author
Papers
Active site electronic structure and dynamics during metalloenzyme catalysis.
TL;DR: This work combines time-resolved X-ray absorption spectroscopy, pre-steady state kinetics and computational quantum chemistry to study the active site zinc ion of bacterial alcohol dehydrogenase during single substrate turnover, detecting a series of alternations in the coordination number and structure.
131
Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2)
Gabriel Rosenblum,Samy O. Meroueh,Oded Kleifeld,Stephen L. Brown,Steven P. Singson,Rafael Fridman,Shahriar Mobashery,Irit Sagi +7 more
TL;DR: A distinct approach is demonstrated for the understanding of the structural mechanism governing the molecular interactions between potent inhibitors and catalytic sites of MMPs, which may aid in the design of effective inhibitors.
45
Spectroscopic studies of inhibited alcohol dehydrogenase from Thermoanaerobacter brockii: proposed structure for the catalytic intermediate state.
TL;DR: The structural and spectroscopic studies indicated that the coordination sphere of the catalytic zinc site in TbADH undergoes conformational changes when it binds the inhibitor and forms a pentacoordinated complex at the zinc ion, providing the first active site structure of bacterial ADH bound to a substrate analogue.
36
Structural characterization of the catalytic active site in the latent and active natural gelatinase B from human neutrophils.
Oded Kleifeld,Philippe E. Van den Steen,Anatoly I. Frenkel,Feng Cheng,Hua-Liang Jiang,Ghislain Opdenakker,Irit Sagi +6 more
TL;DR: The results suggest that the catalytic zinc ion plays a key role in both substrate binding and catalysis in human gelatinase B.
33
Higher metal-ligand coordination in the catalytic site of cobalt-substituted Thermoanaerobacter brockii alcohol dehydrogenase lowers the barrier for enzyme catalysis.
Oded Kleifeld,Lubomoir Rulisek,Oren Bogin,Anatoly I. Frenkel,Zdenek Havlas,Yigal Burstein,Irit Sagi +6 more
TL;DR: It is proposed that the accumulation of a higher coordination number and positive charge at the catalysttic metal ion in TbADH stabilizes the structure of the catalytic transition state and hence lowers the barrier for enzyme catalysis.
28