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Literature summary extracted from

  • Olson, G.J.; Porter, F.D.; Rubinstein, J.; Silver, S.
    Mercuric reductase enzyme from a mercury-volatilizing strain of Thiobacillus ferrooxidans (1982), J. Bacteriol., 151, 1230-1236.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.16.1.1 2-mercaptoethanol thiol compound required, optimal concentration is 0.5 mM Acidithiobacillus ferrooxidans
1.16.1.1 cysteine thiol compound required Acidithiobacillus ferrooxidans
1.16.1.1 dithiothreitol thiol compound required Acidithiobacillus ferrooxidans
1.16.1.1 EDTA required for maximal activity Acidithiobacillus ferrooxidans
1.16.1.1 thioglycolate thiol compound required Acidithiobacillus ferrooxidans

General Stability

EC Number General Stability Organism
1.16.1.1 stable to repeated freeze-thaw cycles Acidithiobacillus ferrooxidans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.1.1 0.015
-
 Hg2+
-
 Acidithiobacillus ferrooxidans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.16.1.1 soluble
-
 Acidithiobacillus ferrooxidans
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.1 Acidithiobacillus ferrooxidans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.1 Hg2+ + NADPH
-
 Acidithiobacillus ferrooxidans Hg + NADP+ + H+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.16.1.1 80
-
 stable at Acidithiobacillus ferrooxidans

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.1 NADPH
-
 Acidithiobacillus ferrooxidans