108 related articles for article (PubMed ID: 1324852)
1. Copper(II)-substituted horse liver alcohol dehydrogenase: structure of the minor species.
Formicka G; Zeppezauer M; Fey F; Hüttermann J
FEBS Lett; 1992 Aug; 309(1):92-6. PubMed ID: 1324852
[TBL] [Abstract][Full Text] [Related]
2. Magnetic and optical properties of copper-substituted alcohol dehydrogenase: a bisthiolate copper (II) complex.
Farrar JA; Formicka G; Zeppezauer M; Thomson AJ
Biochem J; 1996 Jul; 317 ( Pt 2)(Pt 2):447-56. PubMed ID: 8713071
[TBL] [Abstract][Full Text] [Related]
3. An EPR study of the blue copper center in horse liver alcohol dehydrogenase.
Maret W; Zeppezauer M; Desideri A; Morpurgo L; Rotilio G
Biochim Biophys Acta; 1983 Mar; 743(2):200-6. PubMed ID: 6297599
[TBL] [Abstract][Full Text] [Related]
4. Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogue.
Maret W; Zeppezauer M; Sanders-Loehr J; Loehr TM
Biochemistry; 1983 Jun; 22(13):3202-6. PubMed ID: 6349682
[TBL] [Abstract][Full Text] [Related]
5. 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.
Andersson I; Maret W; Zeppezauer M; Brown RD; Koenig SH
Biochemistry; 1981 Jun; 20(12):3424-32. PubMed ID: 7020751
[No Abstract] [Full Text] [Related]
6. Mechanism of aldehyde oxidation catalyzed by horse liver alcohol dehydrogenase.
Olson LP; Luo J; Almarsson O; Bruice TC
Biochemistry; 1996 Jul; 35(30):9782-91. PubMed ID: 8703951
[TBL] [Abstract][Full Text] [Related]
7. Catalytic and spectroscopic characterisation of a copper-substituted alcohol dehydrogenase from yeast.
Vanni A; Anfossi L; Pessione E; Giovannoli C
Int J Biol Macromol; 2002 Mar; 30(1):41-5. PubMed ID: 11893392
[TBL] [Abstract][Full Text] [Related]
8. H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase.
Formicka-Kozłowska G; Schneider-Bernlöhr H; von Wartburg JP; Zeppezauer M
Eur J Biochem; 1988 Apr; 173(2):281-5. PubMed ID: 3360009
[TBL] [Abstract][Full Text] [Related]
9. The binding of 1,10-phenanthroline to specifically active-site cobalt(II)-substituted horse-liver alcohol dehydrogenase. A probe for the open-enzyme conformation.
Sartorius C; Dunn MF; Zeppezauer M
Eur J Biochem; 1988 Nov; 177(3):493-9. PubMed ID: 3197713
[TBL] [Abstract][Full Text] [Related]
10. The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenase.
Bertini I; Lanini G; Luchinat C; Haas C; Maret W; Zeppezauer M
Eur Biophys J; 1987; 14(7):431-9. PubMed ID: 3608931
[TBL] [Abstract][Full Text] [Related]
11. Dissociation of outer-sphere water is rate-limiting for the binding of ligands in the active site of horse liver alcohol dehydrogenase.
Sartorius C; Zeppezauer M
Eur J Biochem; 1988 Nov; 177(3):501-4. PubMed ID: 3197714
[TBL] [Abstract][Full Text] [Related]
12. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.
Piersma SR; Visser AJ; de Vries S; Duine JA
Biochemistry; 1998 Mar; 37(9):3068-77. PubMed ID: 9485460
[TBL] [Abstract][Full Text] [Related]
13. Electronic absorption and EPR spectroscopy of copper alcohol dehydrogenase: pink, violet and green forms of a type 1 copper center analog.
Maret W; Kozłowski H
Biochim Biophys Acta; 1987 Apr; 912(3):329-37. PubMed ID: 3032263
[TBL] [Abstract][Full Text] [Related]
14. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate.
Chen P; Bell J; Eipper BA; Solomon EI
Biochemistry; 2004 May; 43(19):5735-47. PubMed ID: 15134448
[TBL] [Abstract][Full Text] [Related]
15. Copper binding to the prion protein: structural implications of four identical cooperative binding sites.
Viles JH; Cohen FE; Prusiner SB; Goodin DB; Wright PE; Dyson HJ
Proc Natl Acad Sci U S A; 1999 Mar; 96(5):2042-7. PubMed ID: 10051591
[TBL] [Abstract][Full Text] [Related]
16. 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.
Maret W; Dietrich H; Ruf HH; Zeppezauer M
J Inorg Biochem; 1980 Jun; 12(3):241-52. PubMed ID: 6247444
[TBL] [Abstract][Full Text] [Related]
17. Fe(II)-substituted horse liver alcohol dehydrogenase, a model for non-heme iron enzymes. Various states of iron-dioxygen interaction investigated by Mössbauer and EPR spectroscopy.
Bill E; Haas C; Ding XQ; Maret W; Winkler H; Trautwein AX; Zeppezauer M
Eur J Biochem; 1989 Mar; 180(1):111-21. PubMed ID: 2539999
[TBL] [Abstract][Full Text] [Related]
18. Cd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation.
Hemmingsen L; Bauer R; Bjerrum MJ; Zeppezauer M; Adolph HW; Formicka G; Cedergren-Zeppezauer E
Biochemistry; 1995 May; 34(21):7145-53. PubMed ID: 7766625
[TBL] [Abstract][Full Text] [Related]
19. 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.
Schneider-Bernlöhr H; Formicka-Kozłowska G; Bühler R; von Wartburg JP; Zeppezauer M
Eur J Biochem; 1988 Apr; 173(2):275-80. PubMed ID: 3360008
[TBL] [Abstract][Full Text] [Related]
20. Coordination environment of the active-site metal ion of liver alcohol dehydrogenase.
Makinen MW; Yim MB
Proc Natl Acad Sci U S A; 1981 Oct; 78(10):6221-5. PubMed ID: 6273859
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
