Marechal, Amandine and Hartley, Andrew M. and Warelow, Thomas P. and Meunier, B. and Rich, P.R. (2018) Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy. Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (9), pp. 705-711. ISSN 0005-2728.
![[img]](https://eprints.bbk.ac.uk/style/images/fileicons/text.png) |
Text
Accepted Manuscript.pdf - Author's Accepted Manuscript Restricted to Repository staff only Download (682kB) | Request a copy |
|
|
Text
22539a.pdf - Published Version of Record Available under License Creative Commons Attribution. Download (1MB) | Preview |
Abstract
Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736 cm-1 in bovine CcO and previously assigned to D51 is absent from yeast CcO and couldn’t be restored by introduction of a D residue at the equivalent position of the yeast protein. Redox spectra of yeast CcO also show much smaller changes in the amide I region, which may relate to structural differences in the region around D51 and the subunit I/II interface.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | Cytochrome c oxidase, Mitochondria, Infrared spectroscopy, Oxidoreduction, Site-directed mutagenesis, Carboxyl groups |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Dr Amandine Marechal |
| Date Deposited: | 31 May 2018 09:21 |
| Last Modified: | 02 Aug 2023 17:42 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/22539 |
Statistics
Additional statistics are available via IRStats2.
Archive Staff Only (login required)
