Ferredoxin-thioredoxin reductase
| Ferredoxin thioredoxin reductase variable alpha chain | |||||||||
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crystal structure of ferredoxin thioredoxin reductase | |||||||||
| Identifiers | |||||||||
| Symbol | FeThRed_A | ||||||||
| Pfam | PF02941 | ||||||||
| InterPro | IPR004207 | ||||||||
| SCOP2 | 1dj7 / SCOPe / SUPFAM | ||||||||
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| Ferredoxin thioredoxin reductase catalytic beta chain | |||||||||
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crystal structure of ferredoxin thioredoxin reductase | |||||||||
| Identifiers | |||||||||
| Symbol | FeThRed_B | ||||||||
| Pfam | PF02943 | ||||||||
| InterPro | IPR004209 | ||||||||
| SCOP2 | 1dj7 / SCOPe / SUPFAM | ||||||||
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Ferredoxin-thioredoxin reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important role in the ferredoxin/thioredoxin regulatory chain. It catalyzes the following reaction:
- 2 reduced ferredoxin + thioredoxin disulfide 2 oxidized ferredoxin + thioredoxin thiols + 2 H+
Ferredoxin-Thioredoxin reductase (FTR) converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin), regulating enzymes by reduction of specific disulfide groups. It catalyses the light-dependent activation of several photosynthesis enzymes and constitutes the first historical example of a thiol/disulfide exchange cascade for enzyme regulation. It is a heterodimer of subunit alpha and subunit beta. Subunit alpha is the variable subunit, and beta is the catalytic chain. The structure of the beta subunit has been determined and found to fold around the FeS cluster.