Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Johnston, E.M.; Carreira, C.; DellAcqua, S.; Dey, S.G.; Pauleta, S.R.; Moura, I.; Solomon, E.I.
    Spectroscopic definition of the CuZ* intermediate in turnover of nitrous oxide reductase and molecular insight into the catalytic mechanism (2017), J. Am. Chem. Soc., 139, 4462-4476 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.4 additional information
-
 additional information steady-state kinetics, kinetics of reduction of CuZ° versus 1-hole CuZ* Marinobacter nauticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.4 Cu two copper binding sites. The Cu4S active site is ligated by 7 His residues and contains three copper atoms (designated CuI, CuII, and CuIV) that share a plane with the mu4 sulfide ligand and with a solvent-derived ligand that bridges the CuI?CuIV edge, while the fourth copper (CuIII) bound to the mu4S2- is oriented out of this plane. Spectroscopic definition of the resting state of the Cu4S cluster, CuZ* intermediate, in turnover of nitrous oxide. CuZ°, an intermediate form of the Cu4S active site of nitrous oxide reductase (N2OR) is observed in single turnover of fully reduced N2OR with N2O, geometric and electronic structure, overview. CuZ° is a 1-hole (i.e. 3CuICuII) state with spin density delocalized evenly over CuI and CuIV. CuZ° has a terminal hydroxide ligand coordinated to CuIV, stabilized by a hydrogen bond to a nearby lysine residue. CuZ° can be reduced via electron transfer from CuA using a physiologically relevant reductant. Computational modelling of the Cu4S active site built from the atomic coordinates of the crystal structure of PdN2OR, PDB ID 1FWX at 1.6 A resolution, The model includes the active site core (Cu4S), the edge hydroxide, seven ligating histidines, and the second sphere residues Lys397 and Glu435. Spectrocopic Cu binding structure analysis, overview. reduction of CuZ° via electron transfer from CuA in turnover with cytrochrome c552 is faster than the decay of CuZ° to the inactive resting 1-hole CuZ* state of the Cu4S cluster, indicating that N2O reduction by the Cu4S active site of N2OR bypasses the resting 1-hole CuZ* state, which is not reduced by physiologically relevant reductants, instead, the 1-hole CuZ° intermediate is the relevant 1-hole oxidized state of the Cu4S cluster during turnover Marinobacter nauticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.4 nitrous oxide + 2 reduced cytochrome c Marinobacter nauticus
-
 nitrogen + H2O + 2 cytochrome c
-
 ?
1.7.2.4 nitrous oxide + 2 reduced cytochrome c Marinobacter nauticus 617
-
 nitrogen + H2O + 2 cytochrome c
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.4 Marinobacter nauticus Q19Q69
-
-
1.7.2.4 Marinobacter nauticus 617 Q19Q69
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.4 native enzyme is a three-step procedure Marinobacter nauticus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.7.2.4 nitrogen + H2O + 2 ferricytochrome c = nitrous oxide + 2 ferrocytochrome c + 2 H+ spectroscopic definition of the CuZ* intermediate in turnover of nitrous oxide reductase and molecular insight into the catalytic mechanism. The nature of N2O binding and reduction, specifies a molecular mechanism in which N2O coordinates in a mu-1,3 fashion to the fully reduced state, with hydrogen bonding from Lys397, and two electrons are transferred from the fully reduced mu4S2-bridged tetranuclear copper cluster to N2O via a single Cu atom to accomplish N-O bond cleavage Marinobacter nauticus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.7.2.4 culture-condition:nitrate-grown cell
-
 Marinobacter nauticus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.4 nitrous oxide + 2 reduced cytochrome c
-
 Marinobacter nauticus nitrogen + H2O + 2 cytochrome c
-
 ?
1.7.2.4 nitrous oxide + 2 reduced cytochrome c
-
 Marinobacter nauticus 617 nitrogen + H2O + 2 cytochrome c
-
 ?
1.7.2.4 nitrous oxide + 2 reduced methyl viologen
-
 Marinobacter nauticus nitrogen + H2O + 2 methyl viologen
-
 ?
1.7.2.4 nitrous oxide + 2 reduced methyl viologen
-
 Marinobacter nauticus 617 nitrogen + H2O + 2 methyl viologen
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.7.2.4 MhN2OR
-
 Marinobacter nauticus
1.7.2.4 N2OR
-
 Marinobacter nauticus
1.7.2.4 nitrous oxide reductase
-
 Marinobacter nauticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.4 22
-
 assay at room temperature Marinobacter nauticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.2.4 7.6 8 assay at Marinobacter nauticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.4 cytochrome c
-
 Marinobacter nauticus