Pyrococcus furiosus

PS Brereton, FJM Verhagen, ZH Zhou, MWW Adams. Effect of iron-sulfur cluster environment m modulating the thermodynamic properties and biological function of ferredoxm from Pyrococcus furiosus. Biochemistry 37 7351-7362, 1998. 

The molyhdopterin cofactor, as found in different enzymes, may be present either as the nucleoside monophosphate or in the dinucleotide form. In some cases the molybdenum atom binds one single cofactor molecule, while in others, two pterin cofactors coordinate the metal. Molyhdopterin cytosine dinucleotide (MCD) is found in AORs from sulfate reducers, and molyhdopterin adenine dinucleotide and molyb-dopterin hypoxanthine dinucleotide were reported for other enzymes (205). The first structural evidence for binding of the dithiolene group of the pterin tricyclic system to molybdenum was shown for the AOR from Pyrococcus furiosus and D. gigas (199). In the latter, one molyb-dopterin cytosine dinucleotide (MCD) is used for molybdenum ligation. Two molecules of MGD are present in the formate dehydrogenase and nitrate reductase. 

Kjellberg S, M Hermansson, P Marden, GW Jones (1987) The transient phase between growth and nongrowth of heterotrophic bacteria with emphasis on the marine environment. Annu Rev Microbiol 41 25-49. Klump H, J Di Ruggiero, M Kessel, J-B Park, MWW Adams, FT Robb (1992) Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation. J Biol Chem 267 22681-22685. 

Mukund S, MWW Adams (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. J Biol Chem 266 14208-14216. 

Mukund S, MWW Adams (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 270 8389-8392. 

Roy R, S Mukund, GJ Schut, DM Dunn, R Weiss, MWW Adams (1999) Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus the third of a putative five-member tungstoenzyme family. J Bacteriol 181 1171-1180. 

Bevers LE, E Bol, P-L Hagedoorn, WR Hagen (2005) WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity. J Bacteriol 187 7056-7071. 

Roy R, MWW Adams (2002) Characterization of a fourth tungsten-containing enzyme from the hyperthermophilic Pyrococcus furiosus. J Bacterial 184 6952-6956. 

Ferredoxin rednctases in Pyrococcus furiosus inclnding aldehyde ferredoxin reductase, glyceraldehyde-3-phosphate ferredoxin oxidorednctase, and formaldehyde ferredoxin reductase (Roy et al. 1999). 

Hasan MN, Kwakemaak C, Sloof WG, Hagen WR, Heering HA. 2006. Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization. J Biol Inorg Chem 11 651-662. 

NIS measurements have been performed on the rubredoxin (FeSa) type mutant Rm 2-A from Pyrococcus abyssi [103], on Pyrococcus furiosus rubredoxin [104], on Fe2S2 - and Fe4S4 - proteins and model compounds [105, 106], and on the P-cluster and FeMo-cofactor of nitrogenase [105, 107]. 

For example, Fig. 9.40 shows the NIS spectra of the oxidized and reduced FeS4 centers of a rubredoxin mutant from Pyrococcus abyssi obtained at 25 K together with DFT simulations using different models for the Fe-S center [103]. The spectrum from the oxidized protein Fe S4 (S = 5/2) reveals broad bands around 15-25 meV (121-202 cm ) and 42-48 meV (339-387 cm ) consistent with the results on rubredoxin from Pyrococcus furiosus [104]. 

FIGURE 11.9 An extremely broad EPR signal form the superparamagnetic core in ferritin. The spectrum is from Pyrococcus furiosus ferritin. The sharp signal at g = 4.3 (circa 1570 gauss) is from a trace of contaminating dirty iron. ... 

Berrisford, J.M., Hounslow, A.M., Akerboom, J., Hagen, W.R., Brouns, S.J.J., Van der Oost, J., Murray, I.A., Blackburn, G.M., Waltho, J.R, Rice, D.W., and Baker, RJ. 2006. Evidence supporting a cw-enediol-based mechanism for Pyrococcus furiosus phos-phoglucose isomerase. Journal of Molecular Biology 358 1353-1366. 

Tatur, J. and Hagen, W.R. 2005. The dinuclear iron-oxo ferroxidase center of Pyrococcus furiosus ferritin is a stable prosthetic group with unexpectedly high reduction potentials. FEBS Letters 579 4729 1732. 

Two types of SORs have been firstly described by Lombard et al. [44] and Jenney et al. [45]. The first one is a small protein called desulfoferrodoxin (Dfx) found in anaerobic sulfate-reducing bacteria Desulfoarculus baarsii containing two protein domains iron center I and iron center II [44]. Iron center II is supposed to be responsible for the superoxide reducing activity. Another SOR has been isolated from anerobic archaea, Pyrococcus furiosus, which has a unique mononuclear iron center [45], Lombard et al. [46] and Jovanovic et al. [47] also demonstrated that the Treponema pallidum protein of T. pallidum belongs to a new class of SORs. 

Pyrococcus furiosus Archaea 2.10 Candida albicans Fungi 15.0... 

The ability to catalyse the evolution or oxidation of H2 may have been exploited by the earliest life forms as H2 would have been present in the early prebiotic environments. The origins of the proton-dependent chemiosmotic mechanism for ATP synthesis may also reflect the formation of proton gradients created by hydrogenases on either side of the cytoplasmic membrane. In addition, it has been speculated that the coupling of H2 and S metabolisms was also of fundamental importance in the origin of life. These two processes seem intimately coupled in the bifunctional sulfhydrogenase found in Pyrococcus furiosus (a combination of subunits for hydrogenase and sulfite reductase) which can dispose of excess reductant either by the reduction of protons to H2 or S° to H2S (Ma et al. 1993 Pedroni et al. 1995). 

Bryant, F. O. and Adams, M. W. (1989) Characterization of hydrogenase from the hyperther-mophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem., 264, 5070-9. 

Ma, K., Schicho, R. N., Kelly, R. M. and Adams, M. W. W. (1993) Hydrogenase of the hyper-thermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase Evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA, 90, 5341-4. 

Pedroni, P., Della Volpe, A., Galli, G., Mura, G. M., Pratesi, C. and Grandi, G. (1995) Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus Evidence for a relationship to bacterial sulfite reductases. Microbiology, 141, 449-58. 

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