Probes of Hydrogen Tunneling with Horse Liver Alcohol Dehydrogenase at Subzero Temperatures†

Shiou-chuan Tsai; Judith P. Klinman

doi:10.1021/bi002075l

Probes of Hydrogen Tunneling with Horse Liver Alcohol Dehydrogenase at Subzero Temperatures†

Biochemistry ◽

10.1021/bi002075l ◽

2001 ◽

Vol 40 (7) ◽

pp. 2303-2311 ◽

Cited By ~ 30

Author(s):

Shiou-chuan Tsai ◽

Judith P. Klinman

Keyword(s):

Alcohol Dehydrogenase ◽

Hydrogen Tunneling ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Subzero Temperatures ◽

Horse Liver

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Probes of a Role for Remote Binding Interactions on Hydrogen Tunneling in the Horse Liver Alcohol Dehydrogenase Reaction†

Biochemistry ◽

10.1021/bi9920331 ◽

2000 ◽

Vol 39 (6) ◽

pp. 1278-1284 ◽

Cited By ~ 18

Author(s):

Jodie K. Chin ◽

Judith P. Klinman

Keyword(s):

Alcohol Dehydrogenase ◽

Hydrogen Tunneling ◽

Horse Liver Alcohol Dehydrogenase ◽

Binding Interactions ◽

Liver Alcohol Dehydrogenase ◽

Dehydrogenase Reaction ◽

Horse Liver

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Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis

Biochemistry ◽

10.1021/bi00072a003 ◽

1993 ◽

Vol 32 (21) ◽

pp. 5503-5507 ◽

Cited By ~ 86

Author(s):

Brian J. Bahnson ◽

Doo Hong Park ◽

Keehyuk Kim ◽

Bryce V. Plapp ◽

Judith P. Klinman

Keyword(s):

Alcohol Dehydrogenase ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Hydrogen Tunneling ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Dehydrogenase Reaction ◽

Horse Liver

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De Novo design and utilization of photolabile caged substrates as probes of hydrogen tunneling with horse liver alcohol dehydrogenase at sub-zero temperatures: a cautionary note

Bioorganic Chemistry ◽

10.1016/s0045-2068(03)00018-x ◽

2003 ◽

Vol 31 (2) ◽

pp. 172-190 ◽

Cited By ~ 19

Author(s):

Shiou-Chuan Tsai ◽

Judith P. Klinman

Keyword(s):

Alcohol Dehydrogenase ◽

De Novo ◽

De Novo Design ◽

Cautionary Note ◽

Hydrogen Tunneling ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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The binding of NADH to horse liver alcohol dehydrogenase at subzero temperatures. A three-step reaction.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85687-9 ◽

1980 ◽

Vol 255 (8) ◽

pp. 3248-3250

Author(s):

M.A. Greeves ◽

A.L. Fink

Keyword(s):

Alcohol Dehydrogenase ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Subzero Temperatures ◽

Horse Liver

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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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Rate constants for a mechanism including intermediates in the interconversion of ternary complexes by horse liver alcohol dehydrogenase

Biochemistry ◽

10.1021/bi00470a005 ◽

1990 ◽

Vol 29 (18) ◽

pp. 4289-4295 ◽

Cited By ~ 70

Author(s):

V. Chandra Sekhar ◽

Bryce V. Plapp

Keyword(s):

Alcohol Dehydrogenase ◽

Rate Constants ◽

Ternary Complexes ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Synthetic model peptides of the noncatalytic zinc site of EE and SS isozymes of horse liver alcohol dehydrogenase: Interaction with cobalt (II) and nickel (II) ions

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(95)97417-o ◽

1995 ◽

Vol 59 (2-3) ◽

pp. 316

Author(s):

Grazyna Formicka ◽

Ralf Hoffmann ◽

Stephan Rawer ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Horse Liver Alcohol Dehydrogenase ◽

Synthetic Model ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Zinc Site ◽

Model Peptides

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