1.7.2.4: nitrous-oxide reductase

This is an abbreviated version!
For detailed information about nitrous-oxide reductase, go to the full flat file.

Word Map on EC 1.7.2.4

1.7.2.4

denitrification

denitrify

nitrite

greenhouse

denitrificans

paracoccus

stutzeri

dinitrogen

wastewater

binuclear

tetranuclear

cycloclastes

mixed-valence

multicopper

ammonia-oxidizing

n-cycle

nautica

wolinella

arable

nitrospirae

stratospheric

agriculture

t-rflp

degradation

Reaction

+ 2 ferrocytochrome c + 2 H+

Synonyms

cNosZ, EC 1.7.99.6, HdN2OR, McoP, MhN2OR, multicopper oxidase, N(2)OR, N2O reductase, N2OR, nitrous oxide reductase, NosZ, PpN2OR, PsN2OR, Sden_2219, SdN2OR, Z-type N2OR

ECTree

1 Oxidoreductases

1.7 Acting on other nitrogenous compounds as donors

1.7.2 With a cytochrome as acceptor

1.7.2.4 nitrous-oxide reductase

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Results	in table
1	Activating Compound
4524	AA Sequence
4	Application
1	CAS Registry Number
15	Cloned(Commentary)
10	Cofactor
7	Crystallization (Commentary)
5	Expression
20	General Information
3	General Stability
33	Inhibitors
2	kcat/KM [mM/s]
7	Ki Value [mM]
16	KM Value [mM]
12	Localization
64	Metals/Ions
40	Molecular Weight [Da]
77	Natural Substrates/ Products (Substrates)
154	Organism
1	Oxidation Stability
8	Pathway
48	PDB ID
8	pH Optimum
5	pH Range
1	Posttranslational Modification
21	Protein Variants
20	Purification (Commentary)
3	Reaction
3	Reaction Type
116	Reference
3	Source Tissue
38	Specific Activity [micromol/min/mg]
3	Storage Stability
148	Substrates and Products (Substrate)
41	Subunits
154	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
3	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 1.7.2.4 - nitrous-oxide reductase

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additional information

Marinobacter nauticus

the purple form of enzyme, in which the copper centre is in the oxidized [2Cu2+:2Cu+] redox state, is redox active, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the copper centre in either the [1Cu2+:3Cu+] redox state or in the redox inactive state

726100