Ferredoxin thioredoxin reductase: Difference between revisions

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'''Ferredoxin thioredoxin reductase''' (FTR) is a regulatory iron-sulfur enzyme of oxygenic photosynthetic cells .  It catalyzes the 2-electron reduction of the disulfide of thioredoxin (Trx)  with electrons from ferredoxin (Fd).  It contains a catalytic subunit (FTR-C) and variable subunit (FTR-V)<ref>PMID:16245124</ref>.
'''Ferredoxin thioredoxin reductase''' (FTR) is a regulatory iron-sulfur enzyme of oxygenic photosynthetic cells .  It catalyzes the 2-electron reduction of the disulfide of thioredoxin (Trx)  with electrons from ferredoxin (Fd).  It contains a catalytic subunit (FTR-C) and variable subunit (FTR-V)<ref>PMID:16245124</ref>.
<scene name='44/442749/Cv/3'>Ferredoxin thioredoxin reductase catalytic and variable subunits with ferredoxin I with Fe2S2 and Fe4S4</scene> ([[2pvg]]).
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</StructureSection>
== 3D Structures of ferredoxon thioredoxin reductase ==
== 3D Structures of ferredoxon thioredoxin reductase ==

Revision as of 14:12, 17 February 2016


Ferredoxin thioredoxin reductase (FTR) is a regulatory iron-sulfur enzyme of oxygenic photosynthetic cells . It catalyzes the 2-electron reduction of the disulfide of thioredoxin (Trx) with electrons from ferredoxin (Fd). It contains a catalytic subunit (FTR-C) and variable subunit (FTR-V)[1].

(2pvg).

Ferredoxin thioredoxin reductase catalytic (magenta) and variable (green) subunits complex with ferredoxin I (cyan) with Fe2S2 and Fe4S4 clusters 2pvg

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3D Structures of ferredoxon thioredoxin reductase3D Structures of ferredoxon thioredoxin reductase

Updated on 17-February-2016

1dj7 – SyFTR-C +FTR-V – Synechocystis
2pu9 - SyFTR-C +FTR-V+Trx-F (mutant)
2puk - SyFTR-C +FTR-V (mutant)+Trx-M
2puo, 2pvd - SyFTR-C +FTR-V
2pvg - SyFTR-C +FTR-V+Fd-1
2pvo - SyFTR-C +FTR-V+Trx-F + Fd-1

ReferencesReferences

  1. Buchanan BB, Schurmann P, Wolosiuk RA, Jacquot JP. The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth Res. 2002;73(1-3):215-22. PMID:16245124 doi:http://dx.doi.org/10.1023/A:1020407432008

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