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J

John P. Richard

University at Buffalo

H指数:56

被引数:1.0万

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Formate Dehydrogenase: The Role of the AMP Cofactor Fragment in Stabilization of the Transition State for Enzyme-Catalyzed Hydride Transfer

甲酸盐脱氢酶：AMP辅因子片段在酶催化氢转移过渡态稳定化中的作用

IF4.3

2026-04-260

OA

Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NAD+ Cofactor Fragments

酶结构: 磷酸脱氢酶催化的氢化物转移被NAD+辅因子片段激活

IF3

2025-11-010

PRE

The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes

蛋白质侧链在酶活化构象变化中的作用：来自变异酶研究的启示

CHEMICAL REVIEWS

IF55.8

2025-10-011

PRE

Utilization of the NAD Cofactor Binding Energy for Stabilization of Transition States for Enzyme-Catalyzed Hydride Transfer Reactions

JOURNAL OF BIOLOGICAL CHEMISTRY

IF3.9

2023-01-010

OAAI

Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe

ACCOUNTS OF CHEMICAL RESEARCH

IF17.7

2021-05-0310

OAAI

Origin of Free Energy Barriers of Decarboxylation and the Reverse Process of CO2 Capture in Dimethylformamide and in Water (vol 143, pg 137, 2021)

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2021-04-060

PREAI

Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2021-02-0914

OAAI

Origin of Free Energy Barriers of Decarboxylation and the Reverse Process of CO2 Capture in Dimethylformamide and in Water

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2020-12-2917

OA

Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase

IF13.1

2020-09-0315

OAAI

The role of ligand-gated conformational changes in enzyme catalysis

BIOCHEMICAL SOCIETY TRANSACTIONS

IF4.3

2019-10-2816

OAAI

Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Bronsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2019-09-1116

OAAI

Role of the Carboxylate in Enzyme-Catalyzed Decarboxylation of Orotidine 5′-Monophosphate: Transition State Stabilization Dominates Over Ground State Destabilization

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2019-07-3110

OAAI

Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2019-01-3199

OAAI

Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5′-Monophosphate Decarboxylase for Catalysis

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2018-11-2614

OAAI

Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2018-06-0426

OAAI

Orotidine 5′-Monophosphate Decarboxylase: Probing the Limits of the ⁢Possible⁢ for Enzyme Catalysis

ACCOUNTS OF CHEMICAL RESEARCH

IF17.7

2018-03-2936

OAAI

Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2018-03-0829

OAAI

Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes

酶结构: 通过底物诱导的构象变化使活性的Orotidine 5'-单磷酸脱羧酶勃起

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2017-10-2316

OAAI

Charge Transfer Mechanism into the Chevrel Phase Mo6S8 during Mg Intercalation

JOURNAL OF PHYSICAL CHEMISTRY C

IF3.2

2017-08-0742

PREAI

Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

IF15.6

2017-07-1944

OAAI