Literature summary for 1.7.2.4 extracted from

Paraskevopoulos, K.; Antonyuk, S.V.; Sawers, R.G.; Eady, R.R.; Hasnain, S.S.
Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes (2006), J. Mol. Biol., 362, 55-65.

Search for more literature for 1.7.2.4

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion method	Achromobacter cycloclastes

Inhibitors

Inhibitors	Comment	Organism	Structure
sodium iodide	0.2 M	Achromobacter cycloclastes

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu	mu4-sulfide-bridged tetranuclear CuZ cluster	Achromobacter cycloclastes

Organism

Organism	UniProt	Comment	Textmining
Achromobacter cycloclastes	P94127	-	-
Achromobacter cycloclastes 1013	P94127	-	-

Purification (Commentary)

Purification (Comment)	Organism
DEAE cellulose column chromatography, hydroxyapatite column chromatography, Mono Q10 anion-exchange column chromatography, and Sephadex S-200 gel filtration	Achromobacter cycloclastes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.1	-	assayed in the standard dithionite methyl viologen assay	Achromobacter cycloclastes

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N2O + reduced acceptor	-	Achromobacter cycloclastes	N2 + H2O + acceptor	-	?
N2O + reduced acceptor	-	Achromobacter cycloclastes 1013	N2 + H2O + acceptor	-	?

Subunits

Subunits	Comment	Organism
homodimer	x-ray crystallography	Achromobacter cycloclastes

Synonyms

Synonyms	Comment	Organism
N2O reductase	-	Achromobacter cycloclastes
N2OR	-	Achromobacter cycloclastes

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Release 2023.1 (January 2023)