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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cotton, Nick P. J. Jackson, J. Baz Whitehead, Simon J. Veronesi, Giulia Francia, Francesco Giachini, Lisa Boscherini, Federico Venturoli, Giovanni |
| Description | Author Affiliation: Veronesi G ( Dipartimento di Fisica, Università di Bologna, viale C. Berti Pichat 6/2, Bologna, Italy.) |
| Abstract | Transhydrogenase couples hydride transfer between NADH and NADP $^{+}$ to proton translocation across a membrane. The binding of Zn $^{2+}$ to the enzyme was shown previously to inhibit steps associated with proton transfer. Using Zn K-edge X-ray absorption fine structure (XAFS), we report here on the local structure of Zn $^{2+}$ bound to Escherichia coli transhydrogenase. Experiments were performed on wild-type enzyme and a mutant in which βHis91 was replaced by Lys (βH91K). This well-conserved His residue, located in the membrane-spanning domain of the protein, has been suggested to function in proton transfer, and to act as a ligand of the inhibitory Zn $^{2+}$ . The XAFS analysis has identified a Zn $^{2+}$ -binding cluster formed by one Cys, two His, and one Asp/Glu residue, arranged in a tetrahedral geometry. The structure of the site is consistent with the notion that Zn $^{2+}$ inhibits proton translocation by competing with H $^{+}$ binding to the His residues. The same cluster of residues with very similar bond lengths best fits the spectra of wild-type transhydrogenase and βH91K. Evidently, βHis91 is not directly involved in Zn $^{2+}$ binding. The locus of βHis91 and that of the Zn-binding site, although both on (or close to) the proton-transfer pathway of transhydrogenase, are spatially separate. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1797 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2010-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Proteins Chemistry Mutation NADP Transhydrogenases Spectrometry, X-Ray Emission Zinc Amino Acid Substitution Aspartic Acid Genetics Metabolism Binding Sites Cysteine Glutamic Acid Histidine Models, Molecular Protein Binding Protein Structure, Tertiary Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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