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Literature summary for 1.8.1.9 extracted from

  • Walters, E.M.; Garcia-Serres, R.; Jameson, G.N.; Glauser, D.A.; Bourquin, F.; Manieri, W.; Schuermann, P.; Johnson, M.K.; Huynh, B.H.
    Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin:thioredoxin reductase: implications for the catalytic mechanism (2005), J. Am. Chem. Soc., 127, 9612-9624.
    View publication on PubMed
Search for more literature for 1.8.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
C57S inactive mutant containing a redox-active [Fe4S4]3+/2+ center, can be reduced by dithionite Synechocystis sp.
C87A inactive mutant containing a redox-inactive [Fe4S4]2+ cluster Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
[Fe2S2]2+/+
-
 Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thioredoxin + NADP+
-
 Synechocystis sp. thioredoxin disulfide + NADPH
-
 ?

Subunits

Subunits Comment Organism
heterodimer consisting of a highly conserved 13-kDa catalytic subunit, which houses the [Fe4S4] cluster and the adjacent disulfide, and a variable subunit of similar or smaller size, which shows little sequence conservation between species Synechocystis sp.

Synonyms

Synonyms Comment Organism
ferredoxin:thioredoxin reductase
-
 Synechocystis sp.
FTR
-
 Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Synechocystis sp.