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Literature summary for 1.8.5.B1 extracted from

  • Juillan-Binard, C.; Picciocchi, A.; Andrieu, J.P.; Dupuy, J.; Petit-Hartlein, I.; Caux-Thang, C.; Vives, C.; Niviere, V.; Fieschi, F.
    A two-component NADPH oxidase (NOX)-like system in bacteria is involved in the electron transfer chain to the methionine sulfoxide reductase MsrP (2017), J. Biol. Chem., 292, 2485-2494 .
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
H151A mutant has aout 57% of the heme content of wild-type Escherichia coli
H164A mutant has aout 63% of the heme content of wild-type Escherichia coli
H91A almost complete loss of heme binding Escherichia coli


Localization Comment Organism GeneOntology No. Textmining
membrane subunit MsrQ Escherichia coli 16020


Organism UniProt Comment Textmining
Escherichia coli P76342 and P76343 P76342 i.e. catalytic subunit MsrP, P76343 i.e. heme-binding subunit MsrQ

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information subunit MsrQ is reduced due to the free reduced FMN generated by the flavin reductase Fre activity Escherichia coli ?
[protein]-L-methionine + a quinone + H2O
Escherichia coli [protein]-L-methionine (R)-S-oxide + a quinol
[protein]-L-methionine + a quinone + H2O
Escherichia coli [protein]-L-methionine (S)-S-oxide + a quinol


Subunits Comment Organism
More protein physically interacts with flavin reductase Fre Escherichia coli


Synonyms Comment Organism
Escherichia coli
Escherichia coli
protein-methionine-sulfoxide reductase
Escherichia coli


Cofactor Comment Organism Structure
heme heme/protein ratio is 2.5. The extinction coefficient value for the oxidized subunit MsrQ form at 412 nm is 51950 per M and cm. For the reduced MsrQ form at 426 and 558 nm, the extinction coefficient values are 69015 per M and cm and 11075 per M and cm, respectively Escherichia coli