Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases.
atomic force microscopy
flavoproteins
homodimers
protein interactions
redox-active disulfide
single-molecule methods
thioredoxin reductase
Journal
Antioxidants (Basel, Switzerland)
ISSN: 2076-3921
Titre abrégé: Antioxidants (Basel)
Pays: Switzerland
ID NLM: 101668981
Informations de publication
Date de publication:
09 Sep 2021
09 Sep 2021
Historique:
received:
28
07
2021
revised:
02
09
2021
accepted:
06
09
2021
entrez:
28
9
2021
pubmed:
29
9
2021
medline:
29
9
2021
Statut:
epublish
Résumé
Flavin and redox-active disulfide domains of ferredoxin-dependent flavin thioredoxin reductase (FFTR) homodimers should pivot between flavin-oxidizing (FO) and flavin-reducing (FR) conformations during catalysis, but only FR conformations have been detected by X-ray diffraction and scattering techniques. Atomic force microscopy (AFM) is a single-molecule technique that allows the observation of individual biomolecules with sub-nm resolution in near-native conditions in real-time, providing sampling of molecular properties distributions and identification of existing subpopulations. Here, we show that AFM is suitable to evaluate FR and FO conformations. In agreement with imaging under oxidizing condition, only FR conformations are observed for
Identifiants
pubmed: 34573070
pii: antiox10091437
doi: 10.3390/antiox10091437
pmc: PMC8469568
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Agencia Estatal de Investigación
ID : PID2019-103901GB-I00
Organisme : Agencia Estatal de Investigación
ID : PID2019-110900GB-I00
Organisme : Government of Aragón-FEDER
ID : E35_20R
Organisme : Junta de Castilla y León-ERDF "Europe drives our growth"
ID : CLU-2019-05
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