An allosteric redox switch involved in oxygen protection in a CO2 reductase - Archive ouverte HAL Access content directly
Journal Articles Nature Chemical Biology Year : 2024

An allosteric redox switch involved in oxygen protection in a CO2 reductase

Ana Rita Oliveira
Cristiano Mota
  • Function : Author
Guilherme Vilela-Alves
Rita Rebelo Manuel
  • Function : Author
Neide Pedrosa
  • Function : Author
Kateryna Klymanska
  • Function : Author
Maria João Romão
Inês Cardoso Pereira

Abstract

Metal-dependent formate dehydrogenases reduce CO2 with high efficiency and selectivity, but are usually very oxygen sensitive. An exception is Desulfovibrio vulgaris W/Sec-FdhAB, which can be handled aerobically, but the basis for this oxygen tolerance was unknown. Here we show that FdhAB activity is controlled by a redox switch based on an allosteric disulfide bond. When this bond is closed, the enzyme is in an oxygen-tolerant resting state presenting almost no catalytic activity and very low formate affinity. Opening this bond triggers large conformational changes that propagate to the active site, resulting in high activity and high formate affinity, but also higher oxygen sensitivity. We present the structure of activated FdhAB and show that activity loss is associated with partial loss of the metal sulfido ligand. The redox switch mechanism is reversible in vivo and prevents enzyme reduction by physiological formate levels, conferring a fitness advantage during O2 exposure.
Fichier principal
Vignette du fichier
Fdh.pdf (983.58 Ko) Télécharger le fichier
Origin : Files produced by the author(s)

Dates and versions

hal-04383526 , version 1 (09-01-2024)

Identifiers

Cite

Ana Rita Oliveira, Cristiano Mota, Guilherme Vilela-Alves, Rita Rebelo Manuel, Neide Pedrosa, et al.. An allosteric redox switch involved in oxygen protection in a CO2 reductase. Nature Chemical Biology, 2024, 20 (1), pp.111-119. ⟨10.1038/s41589-023-01484-2⟩. ⟨hal-04383526⟩

Collections

CNRS UNIV-AMU ANR
23 View
20 Download

Altmetric

Share

Gmail Facebook X LinkedIn More