A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity

NADPH thioredoxin reductase C (NTRC) is an interesting NTR with a thioredoxin (Trx) domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin (Prx) reduction. NTRC is dimeric in the presence of NADPH and interacted with dimeric 2-Cys Prx through the Trx module by a mixed di...

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Bibliographic Details
Published in:FEBS letters 2009-05, Vol.583 (9), p.1399-1402
Main Authors: Pérez-Ruiz, Juan Manuel, Cejudo, Francisco Javier
Format: Article
Language:English
Subjects:
Catalysis
Chromatography, Gel
Freshwater
Hydrogen peroxide
Mutagenesis, Site-Directed
NADPH thioredoxin reductase
NTR
Oryza - enzymology
Oryza sativa
Peroxiredoxin
Protein Disulfide Reductase (Glutathione) - genetics
Protein Disulfide Reductase (Glutathione) - metabolism
Prx
Reactive oxygen species
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Thioredoxin
Thioredoxin reductase
Thioredoxin-Disulfide Reductase - genetics
Thioredoxin-Disulfide Reductase - metabolism
Trx
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Summary:NADPH thioredoxin reductase C (NTRC) is an interesting NTR with a thioredoxin (Trx) domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin (Prx) reduction. NTRC is dimeric in the presence of NADPH and interacted with dimeric 2-Cys Prx through the Trx module by a mixed disulfide between Cys377 of NTRC and Cys61 of the 2-Cys Prx. NTRC variants of both NTR and Trx active sites were inactive, but 1:1 mixtures of both variants allowed partial recovery of activity suggesting inter-subunit transfer of electrons during catalysis. Based on these results we propose a model for the reaction mechanism of NTRC. MINT- 7017333: 2cys Prx (uniprotkb: Q6ER94) and 2cys Prx (uniprotkb: Q6ER94) bind (MI: 0407) by molecular sieving (MI: 0071) MINT- 7017101, MINT- 7017183: NTRC (uniprotkb: Q70G58) and 2cys Prx (uniprotkb: Q6ER94) bind (MI: 0407) by enzymatic studies (MI: 0415)
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2009.03.067