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Título

Cytochrome c1 exhibits two binding sites for cytochrome c in plants

Autor Moreno-Beltrán, Blas ; Díaz-Quintana, Antonio; González-Arzola, Katiuska ; Velázquez-Campoy, Adrián; Rosa, Miguel A. de la ; Díaz-Moreno, Irene
Palabras clave Respirasome
NMR
Supercomplex
Cytochrome bc1 Complex
Arabidopsis thaliana
Cytochrome c
Fecha de publicación 2014
Citación Biochimica et Biophysica Acta - Bioenergetics 1837: 1717- 1729 (2014)
ResumenIn 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 c1, 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 c1 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. © 2014 Elsevier B.V.
URI http://hdl.handle.net/10261/101716
DOI10.1016/j.bbabio.2014.07.017
Identificadoresdoi: 10.1016/j.bbabio.2014.07.017
issn: 1879-2650
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