Literature summary for 1.7.7.2 extracted from

Rubio, L.M.; Flores, E.; Herrero, A.
Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase (2002), Photosynth. Res., 72, 13-26.

Search for more literature for 1.7.7.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Synechococcus sp.

Protein Variants

Protein Variants	Comment	Organism
C12A	no actiivty, no iron-sulfur cluster	Synechococcus sp.
C16S	1.9% of wild type activity with ferredoxin, no iron-sulfur cluster	Synechococcus sp.
C56A	no activity, no iron-sulfur cluster	Synechococcus sp.
C56S	70% of wild type activity with ferredoxin, contains an iron-sulfur cluster	Synechococcus sp.
C9A	no activity, no iron-sulfur cluster	Synechococcus sp.
C9H	no narB expression	Synechococcus sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	enzyme contains 1 [3Fe-4S] cluster	Synechococcus sp.
Molybdenum	1 atom of Mo and 2 molecules of ribonucleotide-conjugated molybdopterin per molecule of protein	Synechococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
nitrate + reduced ferredoxin	Synechococcus sp.	-	nitrite + H2O + oxidized ferredoxin	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp.	P39458	strain PCC 7942	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Synechococcus sp.

Storage Stability

Storage Stability	Organism
-20°C, 20% glycerol, several months, no loss of activity	Synechococcus sp.
4°C, several weeks, no loss of activity	Synechococcus sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrate + reduced ferredoxin	-	Synechococcus sp.	nitrite + H2O + oxidized ferredoxin	-	?

Synonyms

Synonyms	Comment	Organism
narB	-	Synechococcus sp.

Cofactor

Cofactor	Comment	Organism	Structure
molybdopterin	bis-molybdopterin guanine dinucleotide	Synechococcus sp.

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Release 2023.1 (January 2023)