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Literature summary for 1.7.5.1 extracted from

  • Pinho, D.; Besson, S.; Silva, P.J.; de Castro, B.; Moura, I.
    Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135 (2005), Biochim. Biophys. Acta, 1723, 151-162.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe several iron–sulfur clusters Pseudomonas chlororaphis
Mo the enzyme possesses a molybdopterin guanine dinucleotide active center. Two forms of the molybdenum center, high- and low-pH, are detectable by electron paramagnetic resonance spectroscopy Pseudomonas chlororaphis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
x * 129000 (alpha) + x * 66000 (beta) + x * 24000 (gamma), SDS-PAGE Pseudomonas chlororaphis
66000
-
x * 129000 (alpha) + x * 66000 (beta) + x * 24000 (gamma), SDS-PAGE Pseudomonas chlororaphis
129000
-
x * 129000 (alpha) + x * 66000 (beta) + x * 24000 (gamma), SDS-PAGE Pseudomonas chlororaphis

Organism

Organism UniProt Comment Textmining
Pseudomonas chlororaphis
-
DSM 50135
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas chlororaphis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6
-
-
Pseudomonas chlororaphis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + menaquinol only the membrane-bound, not the solubilized form of the enzyme, can accept electrons from a menaquinone analog, menadione, whereas both forms can accept electrons from methylviologen. In vivo quinol interacts directly with the gamma subunit that is lost during solubilization Pseudomonas chlororaphis nitrite + menaquinone + H2O
-
?
nitrate + reduced methyl viologen
-
Pseudomonas chlororaphis nitrite + oxidized methyl viologen + H2O
-
?

Subunits

Subunits Comment Organism
? x * 129000 (alpha) + x * 66000 (beta) + x * 24000 (gamma), SDS-PAGE Pseudomonas chlororaphis

Cofactor

Cofactor Comment Organism Structure
bis(molybdopterin guanine dinucleotide)molybdenum cofactor the enzyme possesses a molybdopterin guanine dinucleotide active center. Two forms of the molybdenum center, high- and low-pH, are detectable by electron paramagnetic resonance spectroscopy Pseudomonas chlororaphis
cytochrome c the isolated preparation contains heme c in a sub-stoichiometric amount with the ability to relay electrons to the molybdenum center, suggesting that this nitrate reductase may contain heme c instead of the heme b usually found in this class of enzymes Pseudomonas chlororaphis