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Mechanostability of the Single‐Electron‐Transfer Complexes of Anabaena Ferredoxin–NADP + Reductase
Author(s) -
Marcuello Carlos,
de Miguel Rocío,
MartínezJúlvez Marta,
GómezMoreno Carlos,
Lostao Anabel
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201500534
Subject(s) - ferredoxin , ferredoxin—nadp(+) reductase , flavodoxin , chemistry , electron transfer , reductase , nicotinamide adenine dinucleotide phosphate , dissociation (chemistry) , cofactor , oxidoreductase , redox , electron transport chain , photochemistry , crystallography , stereochemistry , enzyme , biochemistry , inorganic chemistry , oxidase test
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.