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Information on EC 1.7.2.5 - nitric oxide reductase (cytochrome c)

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IUBMB Comments
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre comprising a non-heme iron centre and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551
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This record set is specific for:
UNIPROT: Q59646
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nitric oxide reductase, no reductase, p450nor, flavorubredoxin, norcb, nitric-oxide reductase, norbc, no-reductase, ba3-oxidase, nitric oxide reductase cytochrome, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrogen oxide reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
nitrous oxide:ferricytochrome-c oxidoreductase
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre comprising a non-heme iron centre and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551
CAS REGISTRY NUMBER
COMMENTARY hide
37256-43-2
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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
additional information
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all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
nitric oxide reductase subunit C
UniProt
Manually annotated by BRENDA team
nitric oxide reductase subunit C
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NORC_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
146
0
16344
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pisliakov, A.; Hino, T.; Shiro, Y.; Sugita, Y.
Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductase
PLoS Comput. Biol.
8
e1002674
2012
Pseudomonas aeruginosa (Q59646), Pseudomonas aeruginosa ATCC 15692 (Q59646)
Manually annotated by BRENDA team