A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
about
Mathematical and computational modeling in biology at multiple scalesComputational protein engineering: bridging the gap between rational design and laboratory evolution.Characterization of protein contributions to cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase by using photolysis in the ternary complex.Understanding the determinants of selectivity in drug metabolism through modeling of dextromethorphan oxidation by cytochrome P450.Toward accurate screening in computer-aided enzyme design.Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issuesOn catalytic preorganization in oxyanion holes: highlighting the problems with the gas-phase modeling of oxyanion holes and illustrating the need for complete enzyme models.Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase.Interheme electron tunneling in cytochrome c oxidase.The entropic contributions in vitamin B12 enzymes still reflect the electrostatic paradigm.A quantum-chemical picture of hemoglobin affinityStructural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energiesEntropic origin of cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase.Radical Reaction Control in the AdoMet Radical Enzyme CDG Synthase (QueE): Consolidate, Destabilize, AccelerateAdenosylcobalamin enzymes: theory and experiment begin to convergeRelating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.Does compound I vary significantly between isoforms of cytochrome P450?The energetics of the primary proton transfer in bacteriorhodopsin revisited: it is a sequential light-induced charge separation after allGlutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.Electrostatic origin of the catalytic effect of a supramolecular host catalyst.Dynamic, electrostatic model for the generation and control of high-energy radical intermediates by a coenzyme B₁₂-dependent enzyme.The EVB as a quantitative tool for formulating simulations and analyzing biological and chemical reactions.Role of active site residues in promoting cobalt-carbon bond homolysis in adenosylcobalamin-dependent mutases revealed through experiment and computation.An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling.Efficient methylation of C2 in l-tryptophan by the cobalamin-dependent radical S-adenosylmethionine methylase TsrM requires an unmodified N1 amine.Unraveling the Mechanism and Regioselectivity of the B12-Dependent Reductive Dehalogenase PceA.Integrating computational methods to retrofit enzymes to synthetic pathways.The empirical valence bond model: theory and applications
P2860
Q28082151-88A21050-D8C5-4BCC-90A8-6E7ECCF74A8FQ30394571-7C1206B4-084B-4E31-BD89-D74B31AA37E4Q30401832-18DF4E1A-BB70-42B9-9C67-613CB2188E17Q30499595-5F668544-0B06-4A95-8E8B-B184AA13D2B8Q33706085-DA145CFA-0E27-49BA-A73A-BDD54BAE2EF2Q33917537-E8718AB3-5AAF-451D-BF3C-AA77E47BF832Q34154878-D447731F-EF9B-473C-93F6-9CFAD6A458D2Q34165729-7E9CDB08-1AE8-4A7A-A6B9-3F0DCDD3CAB4Q34411065-5FC10A53-9D91-4782-AFBB-6657782946F1Q35377798-9CF196E4-1BC2-4CC1-82F6-5203934314F6Q36276810-6D2D625D-0F7A-49F0-A509-5CFB870F1183Q36283862-C7171AF3-703E-4710-9472-81D88625C50EQ37185158-2C342093-D0D9-4884-BF27-11EA489EE91EQ37340338-215FB11E-09EC-488C-AB96-4E2E2B022C70Q37696590-E34B61B9-0E99-402B-89C2-555C4F215A63Q38003770-2BABA648-342F-464C-B575-9DF0B9D69CCEQ38086666-71593A95-4507-49F3-B3C3-1E09EAD0DDC8Q38562795-71012C62-4738-4446-A65A-65650FA1286AQ39682623-2ACA5D8C-A80A-4558-BADA-27E5F3FF2976Q40031683-6891BDA8-6404-4A97-846A-B157BFE84FB8Q41778737-F2E83A3D-A76E-4A2F-821C-D7081BD887A0Q41865658-9602E65D-1C32-4C22-8EA5-B1A4EC97441CQ41904561-DF25385B-D8D9-40A7-8B62-D677A5A3F06DQ41963377-8E5BC5AE-B1A6-43DC-BD7F-248D654E60BBQ42132462-72DE4CB8-0374-4FDF-9BF8-798C125EA9C5Q48024052-E3DFF7EA-19DB-4562-B27C-2A5C977A3E20Q48055234-987A3EF9-73F3-41EF-9C69-07EF6F85B392Q51531284-951FEC08-CF17-4B94-BD97-5ED38D99ACA9Q58072647-8EACB4A7-62CC-4591-B337-A44A961D4615
P2860
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@ast
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@en
type
label
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@ast
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@en
prefLabel
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@ast
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@en
P2093
P2860
P356
P1476
A new paradigm for electrostatic catalysis of radical reactions in vitamin B12 enzymes.
@en
P2093
Mats H M Olsson
Pankaz K Sharma
Zhen T Chu
P2860
P304
P356
10.1073/PNAS.0702238104
P407
P577
2007-05-21T00:00:00Z