期刊
ANTIOXIDANTS
卷 9, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/antiox9070616
关键词
dimethyl sulfoxide reductase; enzyme kinetics; methionine sulfoxide; oxidative stress; protein oxidation; protein quality control; Rhodobacter sphaeroides
资金
- Commissariat a l'Energie Atomique et aux Energies Alternatives (CEA) [ANR 16-CE11-0012, ANR-16-CE29-0010-01]
- Agence Nationale de la Recherche (ANR) [ANR-16-CE29-0010, ANR-16-CE11-0012] Funding Source: Agence Nationale de la Recherche (ANR)
In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO. Reversible Met oxidation has a wide range of consequences, from protection against oxidative stress to fine-tuned regulation of protein functions. Bacteria distinguish themselves by the production of molybdenum-containing enzymes reducing MetO, such as the periplasmic MsrP which protects proteins during acute oxidative stress. The versatile dimethyl sulfoxide (DMSO) reductases were shown to reduce the free amino acid MetO, but their ability to reduce MetO within proteins was never evaluated. Here, using model oxidized proteins and peptides, enzymatic and mass spectrometry approaches, we showed that theRhodobacter sphaeroidesperiplasmic DorA-type DMSO reductase reduces protein bound MetO as efficiently as the free amino acid L-MetO and with catalytic values in the range of those described for the canonical Msrs. The identification of this fourth type of enzyme able to reduce MetO in proteins, conserved across proteobacteria and actinobacteria, suggests that organisms employ enzymatic systems yet undiscovered to regulate protein oxidation states.
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