Recombinant Thermus thermophilus Ferredoxin--NADP reductase (TT_C0096)
Description
Introduction
Recombinant Thermus thermophilus Ferredoxin--NADP+ reductase (TT_C0096) is an enzyme that belongs to the family of ferredoxin-NADP+ reductases (FNRs). FNRs are oxidoreductases that catalyze the transfer of electrons from ferredoxin to NADP+ in the last step of photosynthetic electron transfer . The enzyme uses FAD as a cofactor and exists as a soluble protein .
Function of Ferredoxin--NADP Reductase
Ferredoxin: NADP+ reductase serves as the terminal enzyme in the electron transfer chain during photosynthesis, specifically transferring electrons from photosystem I to NADPH . The generated NADPH is then essential as a reducing agent in the Calvin cycle reactions . In non-photosynthetic organisms, FNR generally functions in the reverse direction, providing reduced ferredoxin for various metabolic pathways, including nitrogen fixation, terpenoid biosynthesis, steroid metabolism, response to oxidative stress, and the biogenesis of iron-sulfur proteins .
Thermus thermophilus FNR
Thermus thermophilus is a thermophilic bacterium, and its FNR is essential for its metabolism. The FNR from Hydrogenobacter thermophilus TK-6, a thermophilic, obligately chemolithoautotrophic hydrogen-oxidizing bacterium, assimilates carbon dioxide via the reductive tricarboxylic acid cycle . Ferredoxins, which are small iron-sulfur proteins, are vital as low-potential electron donors for this cycle . The fpr gene of H. thermophilus TK-6, which encodes a putative ferredoxin-NADP(+) reductase (FNR, EC 1.18.1.2), was expressed in Escherichia coli, and the recombinant protein was purified to homogeneity . The monomeric Fpr protein contained one molecule of FMN as a prosthetic group and was shown to be a bona fide FNR that catalyzes a reversible redox reaction between NADP(+)/NADPH and ferredoxins .
FNRs in Other Organisms
Bacillus subtilis (YumC) and Rhodopseudomonas palustris CGA009 (RPA3954) FNRs belong to a novel homo-dimeric type of FNR with high amino acid sequence homology to NADPH-thioredoxin reductases . From the Km and kcat values for the diaphorase activity with ferricyanide, it is demonstrated that both FNRs are far more specific for NADPH than for NADH . The UV-visible spectral changes induced by NADP(+) and B. subtilis Fd indicated that both FNRs form a ternary complex with NADP(+) and Fd, and that each of the two ligands decreases the affinities of the others .
Reactions Catalyzed by NfnAB
NfnAB exhibits several activities :
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NAD+-stimulated reduction of TTC with NADPH
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NAD+-dependent reduction of ferredoxin with NADPH
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Ferredoxin-dependent reduction of NAD+ with NADPH
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NADH-dependent reduction of NADP+ with reduced ferredoxin
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Reduction of benzyl viologen with NADPH and NADH
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Oxidation of NADPH and NADH with O2
Table of PDB Accession Codes for FNR Structures
| PDB Accession Codes |
|---|
| 1B2R, 1BJK, 1BQE, 1BX0, 1BX1, 1CJC, 1E1L, 1E62, 1E63, 1E64, 1E6E, 1EWY, 1FDR, 1FNB, 1FNC, 1FND, 1FRN, 1FRQ, 1GAQ, 1GAW, 1GJR, 1GO2, 1GR1, 1H42, 1H85, 1JB9, 1OGI, 1OGJ, 1QFY, 1QFZ, 1QG0, 1QGA, 1QGY, 1QGZ, 1QH0, 1QUE, 1QUF, 1SM4, 1W34, 1W35, 1W87 |
| 2B5O, 2BGI, 2BGJ, 2BMW, 2BSA, 2C7G, 2GQW, 2GR0, 2GR1, 2GR2, 2GR3, 2OK7, 2OK8 |
Product Specs
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