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Binding of ligands to horse liver alcohol dehydrogenase lacking zinc ions at the active sites
| Content Provider | Scilit |
|---|---|
| Author | Kovár, J. Matyska, Luděk Zeppezauer, Michael Maret, Wolfgang Kováň, Jan |
| Copyright Year | 1986 |
| Description | Journal: Journal of Biological Inorganic Chemistry The zinc-deficient enzyme binds the fluorescence probes for the enzyme substrate pocket (auramine O, 13-ethylberberine, chlorprothixene and acridine orange) more tightly than the native enzyme, whereas 1-anilinonaphthalene 8-sulphonic acid is bound with comparable affinity. The use of fluorescence probes as reporter ligands revealed that the formation of binary complexes between the zinc-deficient enzyme and aldehydes is possible (as with the native enzyme) and confirmed an increased affinity of coenzymes to the modified enzyme. The absence of catalytic zinc ions brings about a loss of the essential stabilization effect in simultaneous NADH and aldehyde binding to liver alcohol dehydrogenase. 2,2'-Bipyridine, which chelates the active-site zinc ion in the native enzyme, is bound rather loosely to the same site as aldehydes, auramine O and ethylberberine in the case of the zinc-depleted enzyme. The stopped-flow measurements showed that the pH dependence of auramine O and ethylberberine binding to native and zinc-depleted enzyme is essentially similar. These data are compatible with the presence of ionizable groups in the surroundings of the bound probes. This group might be either His-67, bound to the zinc ion, or the zinc-liganding water molecule in the case of the native enzyme (pK close to 9), or the free His-67 residue in the case of the zinc-deficient enzyme (pK about 8). |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1986.tb09503.x/pdf |
| Ending Page | 396 |
| Page Count | 6 |
| Starting Page | 391 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1986.tb09503.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 2 |
| Volume Number | 155 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1986-03-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Alcohol Dehydrogenase Liver Alcohol Lacking Zinc Dehydrogenase Lacking Ligands To Horse |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
