Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
|Pérez Mejías, Gonzalo
Guerra Castellano, Alejandra
Díaz Quintana, Antonio Jesús
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
|Universidad de Sevilla. Departamento de Biología Vegetal y Ecología
|The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies. Here, we discuss ...
The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies. Here, we discuss three current views-the so-called solid, fluid and plasticity models-which describe the organization of the main membrane-embedded mitochondrial protein complexes and the key elements that regulate and/or facilitate supercomplex assembly. The soluble electron carrier cytochrome c has recently emerged as an essential factor in the assembly and function of respiratory supercomplexes. In fact, a 'restricted diffusion pathway' mechanism for electron transfer between complexes III and IV has been proposed based on the secondary, distal binding sites for cytochrome c at its two membrane partners recently discovered. This channeling pathway facilitates the surfing of cytochrome c on both respiratory complexes, thereby tuning the efficiency of oxidative phosphorylation and diminishing the production of reactive oxygen species. The well-documented post-translational modifications of cytochrome c could further contribute to the rapid adjustment of electron flow in response to changing cellular conditions.
|BFU2015-71017/BMC MINECO/FEDER and PGC2018-096049-B-I00 BIO/BMC MICINN/FEDER, EU
|Pérez Mejías, G., Guerra Castellano, A., Díaz Quintana, A.J., Rosa Acosta, M.Á.d.l. y Díaz Moreno, I. (2019). Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV. Computational and Structural Biotechnology Journal, 17, 654-660.