EurekaMag
+ Translate
+ Most Popular
The pigeon tick (Argas reflexus): its biology, ecology, and epidemiological aspects
Prevalence of hemoglobin abnormalities in Kebili (Tunisian South)
Lipogranuloma: a preventable complication of dacryocystorhinostomy
Value of basal plasma cortisol assays in the assessment of pituitary-adrenal insufficiency
Bees from the Belgian Congo. The acraensis group of Anthophora
Placing gingival retraction cord
Total serum IgE, allergy skin testing, and the radioallergosorbent test for the diagnosis of allergy in asthmatic children
Acariens plumicoles Analgesoidea parasites des oiseaux du Maroc
Injuries of terminal phalanges of the fingers in children
Biology of flowering and nectar production in pear (Pyrus communis)
Das Reliktvorkommen der Aspisviper (Vipera aspis L.) im Schwarzwald
Hydrological modelling of drained blanket peatland
Pathologic morphology and clinical significance of the anomalous origin of the left circumflex coronary artery from the right coronary artery. General review and autopsy analysis of 30 cases
Cyto genetic analyses of lymphocyte cultures after exposure to calcium cyclamate
Axelrodia riesei, a new characoid fish from Upper Rio Meta in Colombia With remarks concerning the genus Axelrodia and description of a similar, sympatric, Hyphessobrycon-species
Favorable evolution of a case of tuberculosis of pancreas under antibiotic action
RIFM fragrance ingredient safety assessment, Valencene, CAS Registry Number 4630-07-3
Parenteral microemulsions: an overview
Temperate pasture: management for grazing and conservation
Evaluation of a new coprocessed compound based on lactose and maize starch for tablet formulation
Thermal expansion and cracking of three confined water-saturated igneous rocks to 800C
Revision of the genera of the tribe Stigmoderini (Coleoptera: Buprestidae) a discussion of phylogenetic relationships
Anal tuberculosis. Report of a case
Gastric tuberculosis in the past and present
Adaptive responses of the cardiovascular system to prolonged spaceflight conditions: assessment with Holter monitoring

Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: a biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitions


Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: a biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitions



Journal of Inorganic Biochemistry 12(3): 241-252



ISSN/ISBN: 0162-0134

PMID: 6247444

DOI: 10.1016/s0162-0134(00)80205-6

Insertion of Cu2+ ions into horse liver alcohol dehydrogenase depleted of its catalytic Zn2+ ions creates an artificial blue copper center similar to that of plastocyanin and similar copper proteins. The esr spectrum of a frozen solution and the optical spectra at 296 and 77 K are reported, together with the corresponding data for binary and ternary complexes with NAD+ and pyrazole. The binary complex of the cupric enzyme with pyrazole establishes a novel type of copper proteins having the optical characteristics of Type 1 and the esr parameters of Type 2 Cu2+. Ternary complex formation with NAD+ converts the Cu2+ ion to a Type 1 center. By an intramolecular redox reaction the cuprous enzyme is formed from the cupric enzyme. Whereas the activity of the cupric alcohol dehydrogenase is difficult to assess (0.5%-1% that of the native enzyme), the cuprous enzyme is distinctly active (8% of the native enzyme). The implications of these findings are discussed in view of the coordination of the metal in native copper proteins.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 042167298

Download citation: RISBibTeXText

Related references

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 dinucleotide. European Journal of Biochemistry 100(1): 267-270, 1979

Ligand binding to the blue copper center of horse liver alcohol dehydrogenase. Febs Letters 136(1): 72-74, 1981

Relation of the auramine O binding site to the active site of horse liver alcohol dehydrogenase. Biochemistry 10(14): 2695-2700, 1971

Chloroprothixene binding into the active site pocket of horse liver alcohol dehydrogenase. Collection of Czechoslovak chemical communications: 76, 41 (3), 1976

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 14(4): 297-311, 1981

Active site specifically reconstituted nickel ii horse liver alcohol dehydrogenase ec 1.1.1.1 optical spectra of binary and ternary complexes with coenzymes coenzyme analogs substrates and inhibitors. Journal of Inorganic Biochemistry 14(4): 297-312, 1981

Site specifically substituted cobalt liver alcohol dehydrogenases part 2 metal ligand interactions in specifically active site substituted cobalt horse liver alcohol dehydrogenase. Hoppe-Seyler's Zeitschrift fuer Physiologische Chemie 359(9): 1074, 1978

Carboxymethylation of horse-liver alcohol dehydrogenase in the crystalline state. The active-site zinc region and general anion-binding site of the enzyme correlated in primary and teritiary structures. European Journal of Biochemistry 58(1): 95-104, 1975

Active-site-specific zinc-depleted and reconstituted cobalt(II) human-liver alcohol dehydrogenase. Preparation, characterization and complexation with NADH and trans-4-(N,N-dimethylamino)-cinnamaldehyde. European Journal of Biochemistry 173(2): 275-280, 1988

Carboxymethylation of horse liver alcohol dehydrogenase ec 1111 in the crystalline state the active site zinc region and general anion binding site of the enzyme correlated in primary and tertiary structures. European Journal Of Biochemistry: 95-104, 1975

Dissociation of outer-sphere water is rate-limiting for the binding of ligands in the active site of horse liver alcohol dehydrogenase. European Journal of Biochemistry 177(3): 501-504, 1988

Purification and properties of a protein component of messenger ribonucleoprotein particles that shares a common epitope with eucaryotic elongation factor Tu. FEBS Journal 173(2): 305-310, 1988

Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme. European Journal of Biochemistry 201(3): 615-625, 1991

The binding of 1,10-phenanthroline to specifically active-site cobalt(II)-substituted horse-liver alcohol dehydrogenase. A probe for the open-enzyme conformation. European Journal of Biochemistry 177(3): 493-499, 1988

Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched acyclic secondary alcohols and ketones as substrates of the native and active site specific cobalt ii substituted enzyme. European Journal of Biochemistry 201(3): 615-626, 1991