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

Wolfgang Maret; Michael Zeppezauer

doi:10.1021/bi00355a020

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

Biochemistry ◽

10.1021/bi00355a020 ◽

1986 ◽

Vol 25 (7) ◽

pp. 1584-1588 ◽

Cited By ~ 21

Author(s):

Wolfgang Maret ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Nicotinamide Adenine Dinucleotide ◽

Metal Ion ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Catalytic Metal

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Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase

Biochemistry ◽

10.1021/bi00320a014 ◽

1984 ◽

Vol 23 (25) ◽

pp. 5982-5996 ◽

Cited By ~ 192

Author(s):

Hans Eklund ◽

Jean Pierre Samama ◽

T. Alwyn Jones

Keyword(s):

Alcohol Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Crystal-structure determination of reduced nicotinamide adenine dinucleotide complex with horse liver alcohol dehydrogenase maintained in its apo conformation by zinc-bound imidazole

Biochemistry ◽

10.1021/bi00294a013 ◽

1983 ◽

Vol 22 (25) ◽

pp. 5761-5772 ◽

Cited By ~ 29

Author(s):

Eila Cedergren-Zeppezauer

Keyword(s):

Crystal Structure ◽

Alcohol Dehydrogenase ◽

Structure Determination ◽

Nicotinamide Adenine Dinucleotide ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Reduced Nicotinamide Adenine Dinucleotide

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The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenase

European Biophysics Journal ◽

10.1007/bf00254867 ◽

1987 ◽

Vol 14 (7) ◽

Cited By ~ 5

Author(s):

I. Bertini ◽

G. Lanini ◽

C. Luchinat ◽

C. Haas ◽

W. Maret ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Metal Ion ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Catalytic Metal

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Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide

Biochemistry ◽

10.1021/bi00414a020 ◽

1988 ◽

Vol 27 (14) ◽

pp. 5082-5088 ◽

Cited By ~ 40

Author(s):

V. Chandra Sekhar ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Horse liver alcohol dehydrogenase-catalyzed oxidation of aldehydes: dismutation precedes net production of reduced nicotinamide adenine dinucleotide

Biochemistry ◽

10.1021/bi00054a001 ◽

1993 ◽

Vol 32 (3) ◽

pp. 735-738 ◽

Cited By ~ 48

Author(s):

Gary T. M. Henehan ◽

Norman J. Oppenheimer

Keyword(s):

Alcohol Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Net Production ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Reduced Nicotinamide Adenine Dinucleotide ◽

Catalyzed Oxidation

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Interaction of chloride ion with horse liver alcohol dehydrogenase-reduced nicotinamide adenine dinucleotide complexes

Biochemistry ◽

10.1021/bi00733a006 ◽

1973 ◽

Vol 12 (9) ◽

pp. 1702-1705 ◽

Cited By ~ 8

Author(s):

Patrick L. Coleman ◽

Henry Weiner

Keyword(s):

Alcohol Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Chloride Ion ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Reduced Nicotinamide Adenine Dinucleotide

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Resonance enhanced Raman identification of the zinc-oxygen bond in a horse liver alcohol dehydrogenase-nicotinamide adenine dinucleotide-aldehyde transient chemical intermediate

Journal of the American Chemical Society ◽

10.1021/ja00391a062 ◽

1981 ◽

Vol 103 (1) ◽

pp. 234-236 ◽

Cited By ~ 17

Author(s):

Paul W. Jagodzinski ◽

Warner L. Peticolas

Keyword(s):

Alcohol Dehydrogenase ◽

Nicotinamide Adenine Dinucleotide ◽

Nicotinamide Adenine ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Oxygen Bond

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Substitutions of a buried glutamate residue hinder the conformational change in horse liver alcohol dehydrogenase and yield a surprising complex with endogenous 3′-Dephosphocoenzyme A

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2018.07.003 ◽

2018 ◽

Vol 653 ◽

pp. 97-106 ◽

Cited By ~ 1

Author(s):

Yun Ho Kim ◽

David S. Gogerty ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(2+) and competition with zinc(2+) and cadmium(2+) ions

Biochemistry ◽

10.1021/bi00515a020 ◽

1981 ◽

Vol 20 (12) ◽

pp. 3433-3438 ◽

Cited By ~ 18

Author(s):

Inger Andersson ◽

Wolfgang Maret ◽

Michael Zeppezauer ◽

Rodney D. Brown ◽

Seymour H. Koenig

Keyword(s):

Alcohol Dehydrogenase ◽

Magnetic Relaxation ◽

Metal Ion ◽

Catalytic Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Ion Substitution ◽

Relaxation Studies

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

Biochemistry ◽

10.1021/bi991731i ◽

1999 ◽

Vol 38 (42) ◽

pp. 13951-13959 ◽

Cited By ~ 56

Author(s):

S. Ramaswamy ◽

Doo-Hong Park ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Conformational Change ◽

Hydrogen Transfer ◽

Horse Liver Alcohol Dehydrogenase ◽

Flexible Loop ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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