Literature summary for 1.7.2.5 extracted from

Oubrie, A.; Gemeinhardt, S.; Field, S.; Marritt, S.; Thomson, A.J.; Saraste, M.; Richardson, D.J.
Properties of a soluble domain of subunit C of a bacterial nitric oxide reductase (2002), Biochemistry, 41, 10858-10865.

Search for more literature for 1.7.2.5

Cloned(Commentary)

Cloned (Comment)	Organism
the water-soluble domain of NorC, cytochrome c type, expressed in Escherichia coli	Paracoccus denitrificans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe	2 heme b, 1 heme c and 1 non-heme	Paracoccus denitrificans
Fe	heme c is six-coordinate, low-spin and in the NorC subunit and NorB contains one six-coordinate, low-spin heme b and a five-coordinate, high-spin heme b3, which, together with a non-heme iron atom, forms the dinuclear NO reduction site	Paracoccus denitrificans
Fe	heme c is bound via an Cys-Xxx-Xxx-Cys-His heme-binding motif	Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 nitric oxide + reduced acceptor	Paracoccus denitrificans	-	nitrous oxide + acceptor + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
water-soluble NorC domain expressed in Escherichia coli	Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 nitric oxide + reduced acceptor	-	Paracoccus denitrificans	nitrous oxide + acceptor + H2O	-	?

Subunits

Subunits	Comment	Organism
dimer	cytochrome bc complex, subunits named NorB and NorC	Paracoccus denitrificans

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Paracoccus denitrificans

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Release 2023.1 (January 2023)