Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases

Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases

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 techni...

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Bibliographic Details
Main Authors: Carlos Marcuello, Gifty Animwaa Frempong, Mónica Balsera, Milagros Medina, Anabel Lostao
Format: Article
Language:English
Published: MDPI AG 2021-09-01
Series:Antioxidants
Subjects:
thioredoxin reductase
atomic force microscopy
protein interactions
redox-active disulfide
single-molecule methods
homodimers
Online Access:https://www.mdpi.com/2076-3921/10/9/1437

Internet

https://www.mdpi.com/2076-3921/10/9/1437

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