5jfc

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NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosusNADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus

Structural highlights

5jfc is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Activity:NAD(P)(+) transhydrogenase (ferredoxin), with EC number 1.6.1.4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.[1] [2] [REFERENCE:4] [SUDHB_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.[3] [4] [5]

References

  1. ↑ Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J Biol Inorg Chem. 2000 Aug;5(4):527-34. PMID:10968624
  2. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401
  3. ↑ Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. J Biol Inorg Chem. 2000 Aug;5(4):527-34. PMID:10968624
  4. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401
  5. ↑ Ma K, Adams MW. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J Bacteriol. 1994 Nov;176(21):6509-17. PMID:7961401

5jfc, resolution 1.60Å

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