000127799 001__ 127799
000127799 005__ 20241125101145.0
000127799 0247_ $$2doi$$a10.3389/fpls.2023.1227492
000127799 0248_ $$2sideral$$a134966
000127799 037__ $$aART-2023-134966
000127799 041__ $$aeng
000127799 100__ $$aTorrado, Alejandro
000127799 245__ $$aPhylogenetic and functional analysis of cyanobacterial Cytochrome c6-like proteins
000127799 260__ $$c2023
000127799 5060_ $$aAccess copy available to the general public$$fUnrestricted
000127799 5203_ $$aAll known photosynthetic cyanobacteria carry a cytochrome c6 protein that acts transferring electrons from cytochrome b6f complex to photosystem I, in photosynthesis, or cytochrome c oxidase, in respiration. In most of the cyanobacteria, at least one homologue to cytochrome c6 is found, the so-called cytochrome c6B or cytochrome c6C. However, the function of these cytochrome c6-like proteins is still unknown. Recently, it has been proposed a common origin of these proteins as well as the reclassification of the cytochrome c6C group as c6B, renaming the new joint group as cytochrome c6BC. Another homologue to cytochrome c6 has not been classified yet, the formerly called cytochrome c6-3, which is present in the heterocyst-forming filamentous cyanobacteria Nostoc sp. PCC 7119. In this work, we propose the inclusion of this group as an independent group in the genealogy of cytochrome c6-like proteins with significant differences from cytochrome c6 and cytochrome c6BC, with the proposed name cytochrome c6D. To support this proposal, new data about phylogeny, genome localisation and functional properties of cytochrome c6-like proteins is provided. Also, we have analysed the interaction of cytochrome c6-like proteins with cytochrome f by isothermal titration calorimetry and by molecular docking, concluding that c6-like proteins could interact with cytochrome b6f complex in a similar fashion as cytochrome c6. Finally, we have analysed the reactivity of cytochrome c6-like proteins with membranes enriched in terminal oxidases of cyanobacteria by oxygen uptake experiments, concluding that cytochrome c6D is able to react with the specific copper-oxidase of the heterocysts, the cytochrome c oxidase 2.
000127799 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000127799 590__ $$a4.1$$b2023
000127799 592__ $$a1.023$$b2023
000127799 591__ $$aPLANT SCIENCES$$b44 / 265 = 0.166$$c2023$$dQ1$$eT1
000127799 593__ $$aPlant Science$$c2023$$dQ1
000127799 594__ $$a7.3$$b2023
000127799 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000127799 700__ $$aIniesta-Pallarés, Macarena
000127799 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000127799 700__ $$aÁlvarez, Consolación
000127799 700__ $$aMariscal, Vicente
000127799 700__ $$aMolina-Heredia, Fernando P.
000127799 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000127799 773__ $$g14 (2023), 227492 [10 pp]$$pFront. plant sci.$$tFrontiers in Plant Science$$x1664-462X
000127799 8564_ $$s8281284$$uhttps://zaguan.unizar.es/record/127799/files/texto_completo.pdf$$yVersión publicada
000127799 8564_ $$s1970875$$uhttps://zaguan.unizar.es/record/127799/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000127799 909CO $$ooai:zaguan.unizar.es:127799$$particulos$$pdriver
000127799 951__ $$a2024-11-22-12:04:00
000127799 980__ $$aARTICLE