The Effect of Temperature, Enzymic Complex Formation on the Room-Temperature Phosphorescence of Tryptophan Residue in Horse Liver Alcohol Dehydrogenase

Yoshiyuki Kai

doi:10.1143/jpsj.48.930

The Effect of Temperature, Enzymic Complex Formation on the Room-Temperature Phosphorescence of Tryptophan Residue in Horse Liver Alcohol Dehydrogenase

Journal of the Physical Society of Japan ◽

10.1143/jpsj.48.930 ◽

1980 ◽

Vol 48 (3) ◽

pp. 930-938

Author(s):

Yoshiyuki Kai

Keyword(s):

Complex Formation ◽

Alcohol Dehydrogenase ◽

Room Temperature ◽

Effect Of Temperature ◽

Tryptophan Residue ◽

Room Temperature Phosphorescence ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Active-Site-Specific Reconstituted Cobalt(II) Horse-Liver Alcohol Dehydrogenase. Changes of the Spectra of the Substrate trans-4-(N,N-Dimethylamino)-cinnamaldehyde and of the Catalytic Cobalt Ion upon Ternary Complex Formation with NADH and 1,4,5,6-Tetrahydronkotinamide-Adenine Dinucleotide

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1979.tb02057.x ◽

1979 ◽

Vol 100 (1) ◽

pp. 267-270 ◽

Cited By ~ 28

Author(s):

Helmut DIETRICH ◽

Wolfgang MARET ◽

Leif WALLEN ◽

Michael ZEPPEZAUER

Keyword(s):

Complex Formation ◽

Alcohol Dehydrogenase ◽

Active Site ◽

Ternary Complex ◽

Horse Liver Alcohol Dehydrogenase ◽

Site Specific ◽

Cobalt Ion ◽

Ternary Complex Formation ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver

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Ternary Complex Formation of Fatty Acids and Fatty Acid Amides with Horse Liver Alcohol Dehydrogenase-Coenzyme Complexes.

Acta Chemica Scandinavica ◽

10.3891/acta.chem.scand.13-1038 ◽

1959 ◽

Vol 13 ◽

pp. 1038-1039 ◽

Cited By ~ 14

Author(s):

Alfred D. Winer ◽

Hugo Theorell ◽

Maie Ojamäe ◽

B. Högberg ◽

P. Kneip ◽

...

Keyword(s):

Fatty Acids ◽

Fatty Acid ◽

Complex Formation ◽

Alcohol Dehydrogenase ◽

Ternary Complex ◽

Horse Liver Alcohol Dehydrogenase ◽

Fatty Acid Amides ◽

Ternary Complex Formation ◽

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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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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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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Further investigations of the transient kinetics of alcohol oxidation catalysed by horse liver alcohol dehydrogenase

Journal of Molecular Biology ◽

10.1016/0022-2836(77)90210-8 ◽

1977 ◽

Vol 114 (2) ◽

pp. 267-279 ◽

Cited By ~ 15

Author(s):

Antonio Baici ◽

Pier Luigi Luisi

Keyword(s):

Alcohol Dehydrogenase ◽

Alcohol Oxidation ◽

Transient Kinetics ◽

Horse Liver Alcohol Dehydrogenase ◽

Liver Alcohol Dehydrogenase ◽

Horse Liver ◽

Kinetics Of

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