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Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ions.

作者信息

Andersson I, Maret W, Zeppezauer M, Brown R D, Koenig S H

出版信息

Biochemistry. 1981 Jun 9;20(12):3424-32. doi: 10.1021/bi00515a019.

DOI:10.1021/bi00515a019
PMID:7020751
Abstract
摘要

相似文献

1
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ions.
Biochemistry. 1981 Jun 9;20(12):3424-32. doi: 10.1021/bi00515a019.
2
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ions.马肝醇脱氢酶催化位点的金属离子取代：溶剂磁弛豫研究结果。2. 锰（II）的结合以及与锌（II）和镉（II）离子的竞争
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Nuclear magnetic resonance studies of substrate interaction with cobalt substituted alcohol dehydrogenase from liver.
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4
Site-specific substituted cobalt(II) horse liver alcohol dehydrogenases. Preparation and characterization in solution, crystalline and immobilized state.
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Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.特定金属缺失和钴取代的马肝醇脱氢酶衍生物活性位点的晶体结构。
Proc Natl Acad Sci U S A. 1983 Sep;80(17):5289-93. doi: 10.1073/pnas.80.17.5289.
6
Metal-directed affinity labeling of zinc(II), cobalt(II), and cadmium(II) horse liver alcohol dehydrogenases.锌（II）、钴（II）和镉（II）马肝醇脱氢酶的金属导向亲和标记
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7
The binding of 1,10-phenanthroline to specifically active-site cobalt(II)-substituted horse-liver alcohol dehydrogenase. A probe for the open-enzyme conformation.1,10-菲咯啉与特异性活性位点钴（II）取代的马肝醇脱氢酶的结合。一种用于开放酶构象的探针。
Eur J Biochem. 1988 Nov 15;177(3):493-9. doi: 10.1111/j.1432-1033.1988.tb14399.x.
8
Influence of anions and pH on the conformational change of horse liver alcohol dehydrogenase induced by binding of oxidized nicotinamide adenine dinucleotide: binding of chloride to the catalytic metal ion.阴离子和pH值对氧化型烟酰胺腺嘌呤二核苷酸结合诱导的马肝醇脱氢酶构象变化的影响：氯离子与催化金属离子的结合
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The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase.钴取代的肝脏乙醇脱氢酶的催化金属原子。
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10
Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase.锌离子、钴离子和镍离子与马肝醇脱氢酶金属缺失催化位点重组的动力学及机制
J Inorg Biochem. 1983 Feb;18(1):59-69. doi: 10.1016/0162-0134(83)85040-5.

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Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.马肝醇脱氢酶：锌配位与催化作用
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3
The coordination of the catalytic zinc in alcohol dehydrogenase studied by combined quantum-chemical and molecular mechanics calculations.
通过量子化学和分子力学联合计算研究乙醇脱氢酶中催化锌的配位情况。
J Comput Aided Mol Des. 1996 Apr;10(2):153-64. doi: 10.1007/BF00402823.
4
Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.特定金属缺失和钴取代的马肝醇脱氢酶衍生物活性位点的晶体结构。
Proc Natl Acad Sci U S A. 1983 Sep;80(17):5289-93. doi: 10.1073/pnas.80.17.5289.