Cd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation

L. Hemmingsen; R. Bauer; M. J. Bjerrum; M. Zeppezauer; H. W. Adolph; G. Formicka; E. Cedergren-Zeppezauer

doi:10.1021/bi00021a028

Cd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation

Biochemistry ◽

10.1021/bi00021a028 ◽

1995 ◽

Vol 34 (21) ◽

pp. 7145-7153 ◽

Cited By ~ 25

Author(s):

L. Hemmingsen ◽

R. Bauer ◽

M. J. Bjerrum ◽

M. Zeppezauer ◽

H. W. Adolph ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Protein Conformation ◽

Catalytic Site ◽

Metal Coordination ◽

Coordination Geometry ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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The Protein Conformation of Cd-Substituted Horse Liver Alcohol Dehydrogenase and its Metal-Site Coordination Geometry in Binary and Ternary Inhibitor Complexes

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1996.00546.x ◽

1996 ◽

Vol 241 (2) ◽

pp. 546-551 ◽

Cited By ~ 16

Author(s):

Lars Hemmingsen ◽

Rogert Bauer ◽

Morten Jannik Bjerrum ◽

Hans Werner Adolph ◽

Michael Zeppezauer ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Protein Conformation ◽

Coordination Geometry ◽

Horse Liver Alcohol Dehydrogenase ◽

Metal Site ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Coordination geometry for cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase: studies by PAC spectroscopy

European Biophysics Journal ◽

10.1007/bf00183458 ◽

1991 ◽

Vol 20 (4) ◽

Cited By ~ 16

Author(s):

R. Bauer ◽

H.W. Adolph ◽

I. Andersson ◽

E. Danielsen ◽

G. Formicka ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Coordination Geometry ◽

Pac Spectroscopy ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Catalytic Zinc ◽

Zinc Site

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Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(83)85040-5 ◽

1983 ◽

Vol 18 (1) ◽

pp. 59-69 ◽

Cited By ~ 9

Author(s):

Gunter Schneider ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Catalytic Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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THE USE OF CHLORIDE ION AS REPORTER GROUP FOR CHANGES IN PROTEIN CONFORMATION. A 35C1 NMR STUDY OF THE BINDING OF COENZYME AND INHIBITORS TO HORSE-LIVER ALCOHOL DEHYDROGENASE

Structure and Function of Oxidation–Reduction Enzymes ◽

10.1016/b978-0-08-016874-6.50071-0 ◽

1972 ◽

pp. 603-611 ◽

Cited By ~ 3

Author(s):

B. LINDMAN ◽

M. ZEPPEZAUER ◽

Å. ÅKESON

Keyword(s):

Alcohol Dehydrogenase ◽

Protein Conformation ◽

Chloride Ion ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Nmr Study ◽

Horse Liver ◽

Reporter Group

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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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Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(2+) and cobalt(2+) ions

Biochemistry ◽

10.1021/bi00515a019 ◽

1981 ◽

Vol 20 (12) ◽

pp. 3424-3432 ◽

Cited By ~ 33

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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Chloroprothixene binding into the active site pocket of horse liver alcohol dehydrogenase

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19760928 ◽

1976 ◽

Vol 41 (3) ◽

pp. 928-940 ◽

Cited By ~ 1

Author(s):

J. Kovář ◽

L. Skurský ◽

K. Bláha

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Active Site Pocket ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)45387-8 ◽

1982 ◽

Vol 257 (23) ◽

pp. 14349-14358 ◽

Cited By ~ 1

Author(s):

H Eklund ◽

B V Plapp ◽

J P Samama ◽

C I Brändén

Keyword(s):

Alcohol Dehydrogenase ◽

Ternary Complex ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compounds.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)42001-2 ◽

1975 ◽

Vol 250 (1) ◽

pp. 205-210

Author(s):

D C Sogin ◽

B V Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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The Behavior of Horse Liver Alcohol Dehydrogenase in Guanidine Hydrochloride Solutions

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)94306-1 ◽

1969 ◽

Vol 244 (18) ◽

pp. 5034-5043

Author(s):

R W Green ◽

R H McKay

Keyword(s):

Alcohol Dehydrogenase ◽

Guanidine Hydrochloride ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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