Fluorinated ligands as NMR probes of active-site nonequivalence in abortive ternary complexes of horse liver alcohol dehydrogenase

D. C. Anderson; M. Lisa Wilson; F. W. Dahlquist

doi:10.1021/bi00262a023

Fluorinated ligands as NMR probes of active-site nonequivalence in abortive ternary complexes of horse liver alcohol dehydrogenase

Biochemistry ◽

10.1021/bi00262a023 ◽

1982 ◽

Vol 21 (19) ◽

pp. 4664-4670 ◽

Cited By ~ 6

Author(s):

D. C. Anderson ◽

M. Lisa Wilson ◽

F. W. Dahlquist

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Ternary Complexes ◽

Horse Liver Alcohol Dehydrogenase ◽

Fluorinated Ligands ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: Optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitors

Journal of Inorganic Biochemistry ◽

10.1016/s0162-0134(00)80287-1 ◽

1981 ◽

Vol 14 (4) ◽

pp. 297-311 ◽

Cited By ~ 24

Author(s):

Helmut Dietrich ◽

Wolfgang Maret ◽

Henryk Kozkłowski ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Optical Spectra ◽

Ternary Complexes ◽

Horse Liver Alcohol Dehydrogenase ◽

Binary And Ternary Complexes ◽

Liver Alcohol Dehydrogenase ◽

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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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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PHOSPHORESCENCE MAXIMA AND TRIPLET STATE LIFETIMES OF NAD + AND ε-NAD+ IN TERNARY COMPLEXES WITH HORSE LIVER ALCOHOL DEHYDROGENASE

Photochemistry and Photobiology ◽

10.1111/j.1751-1097.1989.tb04087.x ◽

1989 ◽

Vol 49 (2) ◽

pp. 137-143 ◽

Cited By ~ 4

Author(s):

KENNETH ROUSSLANG ◽

LYNN ALLEN ◽

J. B. ALEXANDER ROSS

Keyword(s):

Alcohol Dehydrogenase ◽

Triplet State ◽

Ternary Complexes ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Response to Comment on “Effect of Active Site Mutation Phe93 → Trp in the Horse Liver Alcohol Dehydrogenase Enzyme on Catalysis: A Molecular Dynamics Study”

The Journal of Physical Chemistry B ◽

10.1021/jp035474+ ◽

2003 ◽

Vol 107 (44) ◽

pp. 12372-12372 ◽

Cited By ~ 2

Author(s):

Steven D. Schwartz

Keyword(s):

Molecular Dynamics ◽

Alcohol Dehydrogenase ◽

Active Site ◽

Site Mutation ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Dehydrogenase Enzyme

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Active-site cobalt(II)-substituted horse liver alcohol dehydrogenase: characterization of intermediates in the oxidation and reduction processes as a function of pH

Biochemistry ◽

10.1021/bi00377a031 ◽

1987 ◽

Vol 26 (3) ◽

pp. 871-882 ◽

Cited By ~ 31

Author(s):

Christian Sartorius ◽

Martin Gerber ◽

Michael Zeppezauer ◽

Michael F. Dunn

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Reduction Processes ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Comment on “Effect of Active Site Mutation Phe93 → Trp in the Horse Liver Alcohol Dehydrogenase Enzyme on Catalysis: A Molecular Dynamics Study”

The Journal of Physical Chemistry B ◽

10.1021/jp034932b ◽

2003 ◽

Vol 107 (44) ◽

pp. 12370-12371 ◽

Cited By ~ 10

Author(s):

Arieh Warshel ◽

Jordi Villà-Freixa

Keyword(s):

Molecular Dynamics ◽

Alcohol Dehydrogenase ◽

Active Site ◽

Site Mutation ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Dehydrogenase Enzyme

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Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.

The EMBO Journal ◽

10.1002/j.1460-2075.1983.tb01485.x ◽

1983 ◽

Vol 2 (5) ◽

pp. 685-689 ◽

Cited By ~ 21

Author(s):

G. Schneider ◽

H. Eklund ◽

E. Cedergren-Zeppezauer ◽

M. Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Active Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Relation of the auramine O binding site to the active site of horse liver alcohol dehydrogenase

Biochemistry ◽

10.1021/bi00790a006 ◽

1971 ◽

Vol 10 (14) ◽

pp. 2695-2700 ◽

Cited By ~ 15

Author(s):

Ludwig Brand ◽

James R. Heitz

Keyword(s):

Alcohol Dehydrogenase ◽

Binding Site ◽

Active Site ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Auramine O

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Active site specific cadmium(II)-substituted horse liver alcohol dehydrogenase: crystal structures of the free enzyme, its binary complex with NADH, and the ternary complex with NADH and bound p-bromobenzyl alcohol

Biochemistry ◽

10.1021/bi00346a070 ◽

1985 ◽

Vol 24 (25) ◽

pp. 7503-7510 ◽

Cited By ~ 17

Author(s):

Gunter Schneider ◽

Eila Cedergren-Zeppezauer ◽

Stefan Knight ◽

Hans Eklund ◽

Michael Zeppezauer

Keyword(s):

Alcohol Dehydrogenase ◽

Crystal Structures ◽

Active Site ◽

Ternary Complex ◽

Free Enzyme ◽

Binary Complex ◽

Horse Liver Alcohol Dehydrogenase ◽

Site Specific ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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