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1.7.2.5: nitric oxide reductase (cytochrome c)

This is an abbreviated version!
For detailed information about nitric oxide reductase (cytochrome c), go to the full flat file.

Word Map on EC 1.7.2.5

Reaction

nitrous oxide
+
2 ferricytochrome c
+
H2O
= 2 nitric oxide + 2 ferrocytochrome c + 2 H+

Synonyms

Anor, ba3-oxidase, c-type nitric oxide reductase, cNOR, Cnor1, Cnor2, cytochrome c dependent nitric oxide reductase, cytochrome c dependent NOR, cytochrome c type NOR, cytochrome c-dependent nitric oxide reductase, cytochrome c-dependent NO reductase, EC 1.7.99.7, flavorubredoxin, FlRd, Fnor, FprA, membrane-integrated nitric oxide reductase, nitric oxide reductase, nitric oxide reductase cytochrome, nitric oxide-reductase, nitrogen oxide reductase, NO reductase, NO-reductase, NOR, NorB, NorBC, NorC, NorCB, NorZ, P450nor, qCuANOR, respiratory nitric oxide reductase, respiratory NO reductase, S-NOR, scavenging nitric oxide reductase, Tnor

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.2 With a cytochrome as acceptor
                1.7.2.5 nitric oxide reductase (cytochrome c)

Crystallization

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

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at cryogenic temperature -173°C wild-type, S286V- and S286T-mutant
-
in the ferric resting and in the ferrous carbonmonoxy states, at 1.0 and 1.05 A resolution, respectively
-
sitting drop vapour diffusion, crystals diffract to less than 2.0 A
-
in complex with variable heavy chain domain of camel heavy chain antibody, sitting drop vapor diffusion method, using 100 mM potassium phosphate pH 7.0, 0.01% (v/v) phenyl ethanol, 0.005% (v/v) n-dodecyl-beta-D-maltopyranoside
Marinobacter nauticus
-
oxidized S-NOR at 3 A resolution, reduced S-NOR at 2.8 A resolution, NO-reacted S-NOR at 2.8 A resolution
-
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
crystal structure analysis, PDB ID 3O0R