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

scientific article published on June 1, 1980

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 is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/S0162-0134(00)80205-6
P953full work available at URLhttps://api.elsevier.com/content/article/PII:S0162013400802056?httpAccept=text/plain
https://api.elsevier.com/content/article/PII:S0162013400802056?httpAccept=text/xml
P698PubMed publication ID6247444

P2093author name stringM. Zeppezauer
H. Dietrich
H. H. Ruf
W. Maret
P2860cites workProtein measurement with the Folin phenol reagentQ20900776
X-ray crystal structure analysis of plastocyanin at 2.7 Å resolutionQ28314769
Site-Specific Substituted Cobalt(II) Horse Liver Alcohol Dehydrogenases. Preparation and Characterization in Solution, Crystalline and Immobilized StateQ30409267
Spectroscopic studies and a structural model for blue copper centers in proteinsQ34999583
EPR studies on the blue copper protein, rusticyanin: a protein involved in Fe2+ oxidation at pH 2.0 in Thiobacillus ferro-oxidansQ39212963
A crystallographic model for azurin a 3 A resolutionQ39614759
Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenasesQ39645673
Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolutionQ39990970
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-Q40258906
Differences between Alcohol Dehydeogenases. Structural Properties and Evolutionary AspectsQ40750032
Plantacyanin from spinachQ45329836
Conversion of metallothionein into Cu-thionein, the possible low molecular weight form of neonatal hepatic mitochondrocupreinQ47357156
On the state of copper in the blue protein umecyanin.Q50971256
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
alcohol oxidoreductaseQ4713306
inorganic chemistryQ11165
ligand bindingQ61659151
P304page(s)241-252
P577publication date1980-06-01
P1433published inJournal of Inorganic BiochemistryQ3186919
P1476titleActive 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
P478volume12

Reverse relations

cites work (P2860)
Q70177042Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitors
Q36927097Binuclear Cu(A) Formation in Biosynthetic Models of Cu(A) in Azurin Proceeds via a Novel Cu(Cys)2His Mononuclear Copper Intermediate
Q50922712Comparative Cd-113 nuclear magnetic resonance studies of Cd(II)-substituted blue copper proteins
Q45212748Copper(II)-substituted horse liver alcohol dehydrogenase: structure of the minor species
Q30412533Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives
Q36601149Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics
Q36376645Further perspectives on the charge transfer transitions of blue copper proteins and the ligand moieties in stellacyanin
Q50936826Ligand binding to the blue copper center of horse liver alcohol dehydrogenase.
Q42982995Magnetic and optical properties of copper-substituted alcohol dehydrogenase: a bisthiolate copper (II) complex
Q42262610Metal-directed affinity labeling of zinc(II), cobalt(II), and cadmium(II) horse liver alcohol dehydrogenases
Q36317444Normal coordinate analysis of the copper center of azurin and the assignment of its resonance Raman spectrum
Q33866398Pseudomonas stutzeri N2O reductase contains CuA-type sites
Q41892824Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids
Q42167238Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism