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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Baumann, Marc Rauhamäki, Virve Wikström, Mårten Soliymani, Rabah Puustinen, Anne |
| Description | Author Affiliation: Rauhamäki V ( Helsinki Bioenergetics Group, Program for Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Viikinkaari 1, 00014 Helsinki, Finland. virve.rauhamaki@helsinki.fi); |
| Abstract | The heme-copper oxidases constitute a superfamily of terminal dioxygen-reducing enzymes located in the inner mitochondrial or in the bacterial cell membrane. The presence of a mechanistically important covalent bond between a histidine ligand of the copper ion (Cu(B)) in the active site and a generally conserved tyrosine residue nearby has been shown to exist in the canonical cytochrome c oxidases. However, according to sequence alignment studies, this critical tyrosine is missing from the subfamily of cbb(3)-type oxidases found in certain bacteria. Recently, homology modeling has suggested that a tyrosine residue located in a different helix might fulfill this role in these enzymes. Here, we show directly by methods of protein chemistry and mass spectrometry that there is indeed a covalent link between this tyrosine and the copper-ligating histidine. The identity of the cross-linked tyrosine was determined by showing that the cross-link is not formed when this residue is replaced by phenylalanine, even though structural integrity is maintained. These results suggest a universal functional importance of the histidine-tyrosine cross-link in the mechanism of O(2) reduction by all heme-copper oxidases. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 44 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Electron Transport Complex IV Chemistry Metabolism Histidine Rhodobacter Sphaeroides Enzymology Tyrosine Amino Acid Sequence Binding Sites Genetics Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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