Investigation of liver alcohol dehydrogenase catalysis using an NADH biomimetic and comparison with a synthetic zinc model complex-Reference-Cited by-同舟云学术

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Investigation of liver alcohol dehydrogenase catalysis using an NADH biomimetic and comparison with a synthetic zinc model complex

Published:2016-08 Issue: Volume:114 Page:145-151
ISSN:0277-5387
Container-title:Polyhedron
language:en
Short-container-title:Polyhedron

Author:

Sunderland James R.,Tao Xingjian,Butrick Elizabeth E.,Keilich Lauren C.,Villa Christine E.,Miecznikowski John R.,Jain Swapan S.

Funder

Research Corporation

Publisher

Elsevier BV

Subject

Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry

Reference36 articles.

1. Substitutions in a Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer,

2. Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.

3. Biomimetic NAD+ Models for Tandem Cofactor Regeneration, Horse Liver Alcohol Dehydrogenase Recognition of 1,4-NADH Derivatives, and Chiral Synthesis

4. On the Enzymatic Activation of NADH

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1. Engineering Glucose Dehydrogenase to Favor Totally Synthetic Biomimetic Cofactors Containing Carboxyl Group;ChemBioChem;2023-07-12

2. Advanced Insights into Catalytic and Structural Features of the Zinc‐Dependent Alcohol Dehydrogenase from Thauera aromatica;ChemBioChem;2022-06-14

3. SNS donors as mimic to enzymes, chemosensors, and imaging agents;Inorganic Chemistry Communications;2022-02

4. Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase;Journal of Visualized Experiments;2020-03-19

5. Biomimetic cofactors and methods for their recycling;Current Opinion in Chemical Biology;2019-04

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