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Literature summary for 1.7.2.1 extracted from

  • van Wonderen, J.H.; Knight, C.; Oganesyan, V.S.; George, S.J.; Zumft, W.G.; Cheesman, M.R.
    Activation of the cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. Reaction of oxidized enzyme with substrate drives a ligand switch at heme c (2007), J. Biol. Chem., 282, 28207-28215.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state Paracoccus pantotrophus
additional information cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state Pseudomonas stutzeri

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus P72181
-
-
Pseudomonas stutzeri P24040 strain ZoBell ATCC 14405
-
Pseudomonas stutzeri ZoBell / ATCC 14405 P24040 strain ZoBell ATCC 14405
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state Paracoccus pantotrophus ?
-
?
additional information activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction Pseudomonas stutzeri ?
-
?
additional information activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction Pseudomonas stutzeri ZoBell / ATCC 14405 ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Paracoccus pantotrophus
dimer
-
Pseudomonas stutzeri

Synonyms

Synonyms Comment Organism
nitrite reductase
-
Paracoccus pantotrophus
nitrite reductase
-
Pseudomonas stutzeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Pseudomonas stutzeri

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
almost no activity at pH 9.0 Pseudomonas stutzeri

Cofactor

Cofactor Comment Organism Structure
cytochrome cd1 cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine Paracoccus pantotrophus
cytochrome cd1 cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine. Spectral analysis, overview Pseudomonas stutzeri
heme cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer Paracoccus pantotrophus
heme heme c and heme d1, cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer Pseudomonas stutzeri