A theoretical multiscale treatment of protein-protein electron transfer: the ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
10.1016/j.bbabio.2015.09.002
Inclou dades d'ús des de 2022
Cita com:
hdl:2117/84157
Tipus de documentArticle
Data publicació2015-12
EditorElsevier
Condicions d'accésAccés obert
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ProjecteDISENYO COMPUTACIONAL RACIONAL DE OXIDOREDUCTASAS PARA APLICACIONES INDUSTRIALES Y TECNOLOGICAS (MINECO-CTQ2013-48287-R)
SISTEMAS DEPENDIENTES DE FLAVOENZIMAS: DE SUS MECANISMOS DE ACCION A SUS APLICACIONES BIOTECNOLOGICAS Y SANITARIAS (MINECO-BIO2013-42978-P)
SISTEMAS DEPENDIENTES DE FLAVOENZIMAS: DE SUS MECANISMOS DE ACCION A SUS APLICACIONES BIOTECNOLOGICAS Y SANITARIAS (MINECO-BIO2013-42978-P)
Abstract
In the photosynthetic electron transfer (ET) chain, two electrons transfer from photosystem I to the flavin-
dependent ferredoxin-NADP+ reductase (FNR) via two sequential independent ferredoxin (Fd) electron carriers.
In some algae and cyanobacteria (as Anabaena), under low iron conditions, flavodoxin (Fld) replaces Fd as single electron carrier. Extensive mutational studies have characterized the protein–protein interaction in FNR/Fd and
FNR/Fldcomplexes.Interestingly,eventhoughFd and Fldsharethe interaction site on FNR,individual residueson FNR do not participate to the same extent in the interaction with each of the protein partners, pointing to different electron transfer mechanisms. Despite of extensive mutational studies, only FNR/Fd X-ray structures from Anabaena and maize have been solved; structural data for FNR/Fld remains elusive. Here, we present a multiscale modelling approach including coarse-grained and all-atom protein–protein docking, the QM/MM e-Pathway analysis and electronic coupling calculations, allowing for a molecular and electronic comprehensive analysis of the ET process in both complexes. Our results, consistent with experimental mutational data, reveal the ET in FNR/Fd proceeding through a bridge-mediated mechanism in a dominant protein–protein complex, where transfer of the electron is facilitated by Fd loop-residues 40–
49. In FNR/Fld, however, we observe a direct transfer between redox cofactors and less complex specificity than in Fd; more than one orientation in the encounter complex can be efficient in ET.
CitacióSaen-oon, Suwipa [et al.]. A theoretical multiscale treatment of protein-protein electron transfer: the ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems. "Biochimica et Biophysica Acta (BBA) - Bioenergetics", Desembre 2015, vol. 1847, núm. 12, p. 1530-1538.
ISSN0005-2728
Versió de l'editorhttp://www.sciencedirect.com/science/article/pii/S0005272815001905
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