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Information on EC 1.7.2.1 - nitrite reductase (NO-forming) and Organism(s) Homo sapiens

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IUBMB Comments
The reaction is catalysed by two types of enzymes, found in the perimplasm of denitrifying bacteria. One type comprises proteins containing multiple copper centres, the other a heme protein, cytochrome cd1. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. May also catalyse the reaction of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known activity of cytochrome cd1.
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
hemoglobin, cunir, dissimilatory nitrite reductase, marc2, marc1, pseudomonas cytochrome oxidase, cytochrome cd1 nitrite reductase, cu-nir, axnir, cytochrome cd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytochrome c-551:O2, NO2- oxidoreductase
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-
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cytochrome cd
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-
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cytochrome oxidase
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-
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hemoglobin
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mitochondrial amidoxime reducing component
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oxidase, Pseudomonas cytochrome
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Pseudomonas cytochrome oxidase
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reductase, nitrite (cytochrome)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nitric-oxide:ferricytochrome-c oxidoreductase
The reaction is catalysed by two types of enzymes, found in the perimplasm of denitrifying bacteria. One type comprises proteins containing multiple copper centres, the other a heme protein, cytochrome cd1. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. May also catalyse the reaction of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known activity of cytochrome cd1.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-00-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nitrite + ferrocytochrome b5 + 2 H+
nitric oxide + H2O + ferricytochrome b5
show the reaction diagram
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-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
nitrite reduction is catalyzed by molybdenum in the active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tungsten
replacement of molybdenum by tungsten abolishes NO formation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5
nitrite
pH 7.4, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
nitrite
pH 7.4, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
3fold decrease in the rate of NO formation compared to pH 6.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MARC1_HUMAN
337
0
37499
Swiss-Prot
Secretory Pathway (Reliability: 1)
MARC2_HUMAN
335
0
38023
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35000, SDS-PAGE, recombinant His-tagged protein lacking the mitochondrial translocation motif
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C273A
mutation in the putative active site cysteine residue, known to coordinate molybdenum binding. NO formation is abolished by the C273A mutation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and in HEK cell
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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study on use of stabilized hemoglobin as alternative to red cells. Cross-linked hemoglobin bis-tetramers with good oxygen delivery potential have 3fold enhanced nitrite reductase activity, compared to native protein and cross-linked tetramers. Conjugation of four polyethylene glocol chains to the bis-tetramer at each beta-Cys-93 produces a material with additionallly 2.5fold increased nitrite reductase activity while retaining cooperativity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lui, F.E.; Kluger, R.
Enhancing nitrite reductase activity of modified hemoglobin: bis-tetramers and their PEGylated derivatives
Biochemistry
48
11912-11919
2009
Homo sapiens
Manually annotated by BRENDA team
Sparacino-Watkins, C.E.; Tejero, J.; Sun, B.; Gauthier, M.C.; Thomas, J.; Ragireddy, V.; Merchant, B.A.; Wang, J.; Azarov, I.; Basu, P.; Gladwin, M.T.
Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2
J. Biol. Chem.
289
10345-10358
2014
Homo sapiens (Q5VT66), Homo sapiens (Q969Z3), Homo sapiens
Manually annotated by BRENDA team