Mechanostability of the Single-Electron-Transfer Complexes of Anabaena Ferredoxin-NADP+ Reductase
Resumen: The 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.
Idioma: Inglés
DOI: 10.1002/cphc.201500534
Año: 2015
Publicado en: CHEMPHYSCHEM 16, 15 (2015), 3161-3169
ISSN: 1439-4235

Factor impacto JCR: 3.138 (2015)
Categ. JCR: PHYSICS, ATOMIC, MOLECULAR & CHEMICAL rank: 8 / 35 = 0.229 (2015) - Q1 - T1
Categ. JCR: CHEMISTRY, PHYSICAL rank: 50 / 144 = 0.347 (2015) - Q2 - T2

Factor impacto SCIMAGO:

Financiación: info:eu-repo/grantAgreement/ES/DGA/B18
Financiación: info:eu-repo/grantAgreement/ES/MINECO/BIO2013-42978-P
Financiación: info:eu-repo/grantAgreement/ES/MINECO/MAT2012-35358
Tipo y forma: Artículo (Versión definitiva)
Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)

Derechos Reservados Derechos reservados por el editor de la revista

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Artículos > Artículos por área > Bioquímica y Biología Molecular

 Registro creado el 2017-11-30, última modificación el 2018-01-31

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