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Literature summary for 1.7.2.1 extracted from

  • Sam, K.A.; Strampraad, M.J.; de Vries, S.; Ferguson, S.J.
    Very early reaction intermediates detected by microsecond timescale kinetics of cytochrome cd1 catalysed reduction of nitrite (2008), J. Biol. Chem., 283, 27403-27409.
    View publication on PubMed
Search for more literature for 1.7.2.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Paracoccus pantotrophus

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Paracoccus pantotrophus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in the two hemes of cytochrome cd1 Paracoccus pantotrophus

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus P72181
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + H2O + reduced cytochrome cd1 anaerobic assay conditions Paracoccus pantotrophus nitric oxide + H+ + cytochrome cd1
-
 ?

Synonyms

Synonyms Comment Organism
nitrite reductase
-
 Paracoccus pantotrophus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Paracoccus pantotrophus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Paracoccus pantotrophus

pH Range

pH Minimum pH Maximum Comment Organism
6 7
-
 Paracoccus pantotrophus

Cofactor

Cofactor Comment Organism Structure
cytochrome cd1 the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure Paracoccus pantotrophus
heme two hemes in cytochrome cd1, the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure Paracoccus pantotrophus