ExplorEnz: EC 1.8.7.2

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1.8.7.2

Accepted name:

ferredoxin:thioredoxin reductase

Reaction:

2 reduced ferredoxin + thioredoxin disulfide + 2 H⁺ = 2 oxidized ferredoxin + thioredoxin

Systematic name:

ferredoxin:thioredoxin disulfide oxidoreductase

Comments:

The enzyme contains a [4Fe-4S] cluster and internal disulfide. It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers. The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11 (fructose-bisphosphatase), EC 3.1.3.37 (sedoheptulose-bisphosphatase) and EC 2.7.1.19 (phosphoribulokinase) as well as other chloroplast enzymes by disulfide reduction.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Buchanan, B.B. Regulation of CO₂ assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development. Arch. Biochem. Biophys. 288 (1991) 1–9. [DOI] [PMID: 1910303]
2.	Chow, L.P., Iwadate, H., Yano, K., Kamo, M., Tsugita, A., Gardet-Salvi, L., Stritt-Etter, A.L. and Schurmann, P. Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster. Eur. J. Biochem. 231 (1995) 149–156. [DOI] [PMID: 7628465]
3.	Staples, C.R., Ameyibor, E., Fu, W., Gardet-Salvi, L., Stritt-Etter, A.L., Schurmann, P., Knaff, D.B. and Johnson, M.K. The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters. Biochemistry 35 (1996) 11425–11434. [DOI] [PMID: 8784198]

[EC 1.8.7.2 created 2010, modified 2023]