000063358 001__ 63358
000063358 005__ 20180131144955.0
000063358 0247_ $$2doi$$a10.1002/cphc.201500534
000063358 0248_ $$2sideral$$a92863
000063358 037__ $$aART-2015-92863
000063358 041__ $$aeng
000063358 100__ $$0(orcid)0000-0003-3459-8605$$aMarcuello, C.
000063358 245__ $$aMechanostability of the Single-Electron-Transfer Complexes of Anabaena Ferredoxin-NADP+ Reductase
000063358 260__ $$c2015
000063358 5060_ $$aAccess copy available to the general public$$fUnrestricted
000063358 5203_ $$aThe complexes formed between the flavoenzyme ferredoxin-NADP+ reductase (FNR; NADP+=nicotinamide adenine dinucleotide phosphate) and its redox protein partners, ferredoxin (Fd) and flavodoxin (Fld), have been analysed by using dynamic force spectroscopy through AFM. A strategy is developed to immobilise proteins on a substrate and AFM tip to optimise the recognition ability. The differences in the recognition efficiency regarding a random attachment procedure, together with nanomechanical results, show two binding models for these systems. The interaction of the reductase with the natural electron donor, Fd, is threefold stronger and its lifetime is longer and more specific than that with the substitute under iron-deficient conditions, Fld. The higher bond probability and two possible dissociation pathways in Fld binding to FNR are probably due to the nature of this complex, which is closer to a dynamic ensemble model. This is in contrast with the one-step dissociation kinetics that has been observed and a specific interaction described for the FNR:Fd complex.
000063358 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B18$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2013-42978-P$$9info:eu-repo/grantAgreement/ES/MINECO/MAT2012-35358
000063358 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000063358 590__ $$a3.138$$b2015
000063358 591__ $$aPHYSICS, ATOMIC, MOLECULAR & CHEMICAL$$b8 / 35 = 0.229$$c2015$$dQ1$$eT1
000063358 591__ $$aCHEMISTRY, PHYSICAL$$b50 / 144 = 0.347$$c2015$$dQ2$$eT2
000063358 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000063358 700__ $$aDe Miguel, R.
000063358 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, M.$$uUniversidad de Zaragoza
000063358 700__ $$aGómez-Moreno, C.
000063358 700__ $$0(orcid)0000-0001-7460-5916$$aLostao, A.$$uUniversidad de Zaragoza
000063358 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDepartamento de Bioquímica y Biología Molecular y Celular$$cBioquímica y Biología Molecular
000063358 773__ $$g16, 15 (2015), 3161-3169$$pChemphyschem$$tCHEMPHYSCHEM$$x1439-4235
000063358 8564_ $$s575128$$uhttps://zaguan.unizar.es/record/63358/files/texto_completo.pdf$$yVersión publicada
000063358 8564_ $$s130499$$uhttps://zaguan.unizar.es/record/63358/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000063358 909CO $$ooai:zaguan.unizar.es:63358$$particulos$$pdriver
000063358 951__ $$a2018-01-31-14:32:53
000063358 980__ $$aARTICLE