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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Wilson, Michael T. Nicholls, Peter Silkstone, Gary G. Rajagopal, Badri S. Worrall, Jonathan A. R. |
| Description | Author Affiliation: Rajagopal BS ( School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK.) |
| Abstract | Mitochondrial cytochrome c associates with the phosphoplipid cardiolipin (CL) through a combination of electrostatic and hydrophobic interactions. The latter occurs by insertion into cytochrome c of an acyl chain, resulting in the dissociation of the axial Met-80 heme-iron ligand. The resulting five coordinate cytochrome c /CL complex has peroxidatic properties leading to peroxidation of CL and dissociation of the complex. These events are considered to be pre-apoptotic and culminate with release of cytochrome c from the mitochondria into the cytoplasm. Two distinct surface regions on cytochrome c have been suggested to mediate CL acyl chain insertion and this study has probed one of these regions. We have constructed a series of alanine mutants aimed at disrupting a surface cleft formed between residues 67–71 and 82–85. The physicochemical properties, peroxidase activity, CL binding, and kinetics of carbon monoxide (CO) binding to the ferrous cytochrome c /CL complex have been assessed for the individual mutants. Our findings reveal that the majority of mutants are capable of binding CL in the same apparent stoichiometry as the wild-type protein, with the extent to which the Met-80 ligand is bound in the ferrous cytochrome c /CL complex being mutant specific at neutral pH. Mutation of the species conserved Arg-91 residue, that anchors the cleft, results in the greatest changes to physicochemical properties of the protein leading to a change in the CL binding ratio required to effect structural changes and to the ligand-exchange properties of the ferrous cytochrome c /CL complex. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 5 |
| Volume Number | 1817 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-05-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Cardiolipins Metabolism Cytochromes c Saccharomyces Cerevisiae Acylation Animals Carbon Monoxide Circular Dichroism Hydrogen-Ion Concentration Kinetics Lasers Models, Biological Mutant Proteins Oxidation-Reduction Peroxidase Photolysis Protein Binding Spectrum Analysis Time Factors Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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