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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Angerer, Heike Michel, Hartmut Koepke, Juergen Müller, Hannelore Olkhova, Elena Peng, Guohong |
| Description | Author Affiliation: Koepke J ( Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Max-von-Laue-Str.3, D-60438 Frankfurt/Main, Germany.) |
| Abstract | The structure of the two-subunit cytochrome c oxidase from Paracoccus denitrificans has been refined using X-ray cryodata to 2.25 Å resolution in order to gain further insights into its mechanism of action. The refined structural model shows a number of new features including many additional solvent and detergent molecules. The electron density bridging the heme $a_{3}$ iron and Cu $_{B}$ of the active site is fitted best by a peroxo-group or a chloride ion. Two waters or OH $^{−}$ groups do not fit, one water (or OH $^{−}$ ) does not provide sufficient electron density. The analysis of crystals of cytochrome c oxidase isolated in the presence of bromide instead of chloride appears to exclude chloride as the bridging ligand. In the D-pathway a hydrogen bonded chain of six water molecules connects Asn131 and Glu278, but the access for protons to this water chain is blocked by Asn113, Asn131 and Asn199. The K-pathway contains two firmly bound water molecules, an additional water chain seems to form its entrance. Above the hemes a cluster of 13 water molecules is observed which potentially form multiple exit pathways for pumped protons. The hydrogen bond pattern excludes that the Cu $_{B}$ ligand His326 is present in the imidazolate form. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 6 |
| Volume Number | 1787 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2009-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Metabolism Electron Transport Complex IV Paracoccus Denitrificans Enzymology Catalytic Domain Crystallography, X-Ray Heme Hydrogen Bonding Models, Biological Models, Molecular Protein Conformation Protons Static Electricity Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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