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Literature summary for 1.16.1.1 extracted from

  • Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
    Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study (2018), Eur. Biophys. J., 47, 205-223 .
    View publication on PubMed
Search for more literature for 1.16.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Enterococcus faecalis
gene merA, recombinant expression in Escherichia coli strain CM037 harbouring the Tn4378 transposon which contains a mer operon of Rm CH34 Cupriavidus metallidurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hg2+ + NADPH Cupriavidus metallidurans
-
 Hg + NADP+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Cupriavidus metallidurans
-
 i.e. Cupriavidus metallidurans
-
Enterococcus faecalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant MerA from Escherichia coli strain CM037 Cupriavidus metallidurans

Reaction

Reaction Comment Organism Reaction ID
Hg + NADP+ + H+ = Hg2+ + NADPH catalytic mechanisms of the flavoprotein MerA, overview Cupriavidus metallidurans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg2+ + NADPH
-
 Cupriavidus metallidurans Hg + NADP+ + H+
-
 ?

Synonyms

Synonyms Comment Organism
MerA
-
 Enterococcus faecalis
MerA
-
 Cupriavidus metallidurans
mercuric ion reductase
-
 Cupriavidus metallidurans
Rm CH34
-
 Cupriavidus metallidurans

Cofactor

Cofactor Comment Organism Structure
FAD a flavoprotein, spectral analysis of the binding structure and environment, overview Cupriavidus metallidurans
FAD flavoprotein. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts Enterococcus faecalis
additional information each monomer contains a FAD and a redoxactive disulfide group close to the FAD isoalloxazine ring. MerA has an additional Cys/Cys redox site in the C-terminal part of its sequence Cupriavidus metallidurans
NADPH
-
 Cupriavidus metallidurans

General Information

General Information Comment Organism
additional information the resonance Raman (RR) spectra of various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts Cupriavidus metallidurans
physiological function the enzyme catalyzes the reduction and detoxification of toxic mercuric ion, it reduces the Hg(II) ion to the less toxic elemental mercury (Hg(0)) using NADPH as a source of reducing power Cupriavidus metallidurans