期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1859, 期 9, 页码 705-711出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2018.05.018
关键词
Cytochrome c oxidase; Mitochondria; Infrared spectroscopy; Oxidoreduction; Site-directed mutagenesis; Carboxyl groups
资金
- Medical Research Council UK (Career Development Award) [MR/M00936X/1]
- Birkbeck Wellcome Trust Institutional Strategic Support Fund [105628/Z/14/Z]
- Biotechnology and Biological Sciences Research Council UK [BB/K001094/1]
- Wellcome Trust [105628/Z/14/Z] Funding Source: Wellcome Trust
- BBSRC [BB/K001094/1, BB/H000097/1] Funding Source: UKRI
- MRC [MR/M00936X/1] Funding Source: UKRI
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.
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