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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | González-arzola, Katiuska Díaz-moreno, Irene Velázquez-campoy, Adrián Moreno-beltrán, Blas De La Rosa, Miguel A. Díaz-quintana, Antonio |
| Description | Author Affiliation: Moreno-Beltrán B ( Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla - CSIC, Avda. Américo Vespucio 49, Sevilla 41092, Spain.); Díaz-Quintana A ( Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla - CSIC, Avda. Américo Vespucio 49, Sevilla 41092, Spain.); González-Arzola K ( Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla - CSIC, Avda. Américo Vespucio 49, Sevilla 41092, Spain.); Velázquez-Campoy A ( Institute of Biocomputation and Physics of Complex Systems (BIFI)-Joint Unit BIFI-IQFR (CSIC), Universidad de Zaragoza, Mariano Esquillor s/n, 50018, Zaragoza, Spain); De la Rosa MA ( Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla - CSIC, Avda. Américo Vespucio 49, Sevilla 41092, Spain.); Díaz-Moreno I ( Instituto de Bioquímica Vegetal y Fotosíntesis, cicCartuja, Universidad de Sevilla - CSIC, Avda. Américo Vespucio 49, Sevilla 41092, Spain. Electronic address: idiazmoreno@us.es.) |
| Abstract | In plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c behaves inside a supercomplex such as the respirasome, formed by complexes I, III and IV, remains obscure from a structural point of view. Here, we report ab-initio Brownian dynamics calculations and nuclear magnetic resonance-driven docking computations showing two binding sites for plant cytochrome c at the head soluble domain of plant cytochrome $c_{1}$ , namely a non-productive (or distal ) site with a long heme-to-heme distance and a functional (or proximal ) site with the two heme groups close enough as to allow electron transfer. As inferred from isothermal titration calorimetry experiments, the two binding sites exhibit different equilibrium dissociation constants, for both reduced and oxidized species, that are all within the micromolar range, thus revealing the transient nature of such a respiratory complex. Although the docking of cytochrome c at the distal site occurs at the interface between cytochrome $c_{1}$ and the Rieske subunit, it is fully compatible with the complex III structure. In our model, the extra distal site in complex III could indeed facilitate the functional cytochrome c channeling towards complex IV by building a “floating boat bridge” of cytochrome c molecules (between complexes III and IV) in plant respirasome. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 10 |
| Volume Number | 1837 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-10-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Cytochromes C1 Metabolism Plants Enzymology Binding Sites Genetics DNA Primers Magnetic Resonance Spectroscopy Molecular Docking Simulation Mutagenesis, Site-Directed Polymerase Chain Reaction Ultracentrifugation Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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