Literature summary for 1.7.2.1 extracted from

Allen, J.W.; Higham, C.W.; Zajicek, R.S.; Watmough, N.J.; Ferguson, S.J.
A novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1 (2002), Biochem. J., 366, 883-888.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
NO2- + reduced cytochrome c550	Paracoccus pantotrophus	unambiguously identified as physiological electron donor	NO + oxidized cytochrome c550	-	?
NO2- + reduced pseudoazurin	Paracoccus pantotrophus	unambiguously identified as physiological electron donor	NO + oxidized pseudoazurin	-	?

Organism

Organism	UniProt	Comment	Textmining
Paracoccus pantotrophus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Paracoccus pantotrophus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NH2OH + reduced cytochrome c550	additional electron donor: horse heart cytochrome c	Paracoccus pantotrophus	NH3 + H2O + oxidized cytochrome c550	-	?
NO2- + reduced cytochrome c550	unambiguously identified as physiological electron donor	Paracoccus pantotrophus	NO + oxidized cytochrome c550	-	?
NO2- + reduced pseudoazurin	unambiguously identified as physiological electron donor	Paracoccus pantotrophus	NO + oxidized pseudoazurin	-	?

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Release 2023.1 (January 2023)