COORDINATION CHEMISTRY AND FUNCTION OF THE CATALYTIC METAL-ION IN LIVER ALCOHOL-DEHYDROGENASE

[1] ABDALLAH MA, BIOCHEMISTRY

[2] METAL-ION SUBSTITUTION AT THE CATALYTIC SITE OF HORSE-LIVER ALCOHOL-DEHYDROGENASE - RESULTS FROM SOLVENT MAGNETIC-RELAXATION STUDIES .1. COPPER(II) AND COBALT(II) IONS [J]. BIOCHEMISTRY, 1981, 20 (12) : 3424 - 3432

[3] ANDERSSON I, 1982, INORG CHIM A-BIOINOR, V67, P53

[4] ANDERSSON I, 1980, BIOCHEMISTRY, V20, P3433

[5] EFFECT OF NADH ON THE PKA OF ZINC-BOUND WATER IN LIVER ALCOHOL-DEHYDROGENASE [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1981, 113 (03): : 425 - 433

[6] BERTINI I, J AM CHEM SOC

[7] Branden C-I., 1975, ENZYMES, V11, P103, DOI 10.1016/S1874-6047(08)60211-5

[8] CRYSTAL-STRUCTURE DETERMINATIONS OF CO-ENZYME ANALOG AND SUBSTRATE COMPLEXES OF LIVER ALCOHOL-DEHYDROGENASE - BINDING OF 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE-DINUCLEOTIDE AND TRANS-4-(N,N-DIMETHYLAMINO)CINNAMALDEHYDE TO THE ENZYME [J]. BIOCHEMISTRY, 1982, 21 (20) : 4895 - 4908

[9] ACTIVE SITE-SPECIFICALLY RECONSTITUTED NICKEL(II) HORSE LIVER ALCOHOL-DEHYDROGENASE - OPTICAL-SPECTRA OF BINARY AND TERNARY COMPLEXES WITH COENZYMES, COENZYME ANALOGS, SUBSTRATES, AND INHIBITORS [J]. JOURNAL OF INORGANIC BIOCHEMISTRY, 1981, 14 (04) : 297 - 311

[10] 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-TETRAHYDRONICOTINAMIDE-ADENINE DINUCLEOTID [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1979, 100 (01): : 267 - 270

[1] ABDALLAH MA, BIOCHEMISTRY

[2] METAL-ION SUBSTITUTION AT THE CATALYTIC SITE OF HORSE-LIVER ALCOHOL-DEHYDROGENASE - RESULTS FROM SOLVENT MAGNETIC-RELAXATION STUDIES .1. COPPER(II) AND COBALT(II) IONS [J]. BIOCHEMISTRY, 1981, 20 (12) : 3424 - 3432

[3] ANDERSSON I, 1982, INORG CHIM A-BIOINOR, V67, P53

[4] ANDERSSON I, 1980, BIOCHEMISTRY, V20, P3433

[5] EFFECT OF NADH ON THE PKA OF ZINC-BOUND WATER IN LIVER ALCOHOL-DEHYDROGENASE [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1981, 113 (03): : 425 - 433

[6] BERTINI I, J AM CHEM SOC

[7] Branden C-I., 1975, ENZYMES, V11, P103, DOI 10.1016/S1874-6047(08)60211-5

[8] CRYSTAL-STRUCTURE DETERMINATIONS OF CO-ENZYME ANALOG AND SUBSTRATE COMPLEXES OF LIVER ALCOHOL-DEHYDROGENASE - BINDING OF 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE-DINUCLEOTIDE AND TRANS-4-(N,N-DIMETHYLAMINO)CINNAMALDEHYDE TO THE ENZYME [J]. BIOCHEMISTRY, 1982, 21 (20) : 4895 - 4908

[9] ACTIVE SITE-SPECIFICALLY RECONSTITUTED NICKEL(II) HORSE LIVER ALCOHOL-DEHYDROGENASE - OPTICAL-SPECTRA OF BINARY AND TERNARY COMPLEXES WITH COENZYMES, COENZYME ANALOGS, SUBSTRATES, AND INHIBITORS [J]. JOURNAL OF INORGANIC BIOCHEMISTRY, 1981, 14 (04) : 297 - 311

[10] 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-TETRAHYDRONICOTINAMIDE-ADENINE DINUCLEOTID [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1979, 100 (01): : 267 - 270