| Autor: |
Oliveira, Ana Rita, Mota, Cristiano, Vilela-Alves, Guilherme, Manuel, Rita Rebelo, Pedrosa, Neide, Fourmond, Vincent, Klymanska, Kateryna, Léger, Christophe, Guigliarelli, Bruno, Romão, Maria João, Cardoso Pereira, Inês A. |
| Zdroj: |
Nature Chemical Biology; 20230101, Issue: Preprints p1-9, 9p |
| Abstrakt: |
Metal-dependent formate dehydrogenases reduce CO2with high efficiency and selectivity, but are usually very oxygen sensitive. An exception is Desulfovibrio vulgarisW/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 O2exposure. |
| Databáze: |
Supplemental Index |
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