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Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase

Antioxidants (Basel). 2020; 
Lionel Tarrago, Sandrine Grosse, David Lemaire, Laetitia Faure, Mathilde Tribout, Marina I Siponen, Mila Kojadinovic-Sirinelli, David Pignol, Pascal Arnoux, Monique Sabaty
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Peptide Synthesis … Protein solution was desalted using PD MiniTrap G-10 (GE Healthcare) in 50 mM MOPS, 150 mM NaCl, pH 7.5, and concentrated. QWGAGM(O)QAEED and TTPGYM(O)EEWNK peptides were obtained from GenScript ® (Hong-Kong) … Get A Quote

摘要

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... More

关键词

Rhodobacter sphaeroides, dimethyl sulfoxide reductase, enzyme kinetics, methionine sulfoxide, oxidative stress, protein oxidation, protein quality control
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