Pyrococcus

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]. 

Fig. 9.40 NIS spectra of oxidized (filled circle) and reduced rubredoxin mutant Rm 2-4 (filled triangle) from Pyrococcus abyssi obtained at 25 K. The protein samples have been prepared with Fe concentrations of about 10 mM. Theoretically calculated NIS spectra based on DFT calculations (B3LYP/CEP-3IG) of 9, 21 and 49 atoms are shown below. The dotted lines represent calculated NIS spectra for the oxidized Fe S4 center and the dashed lines for the reduced Fe°S4 center. (Taken from [103])...

A nitrilase from the hyperthermophile Pyrococcus abyssi, which exhibits optimal growth at 100 °C, was cloned and overexpressed. Characterization of this nitrilase revealed that it is operational as a dimer (rather than the more common multimeric structure for nitrilases), with optimal pH at 7.4 and optimal apparent activity at 80 °C with Tm (DSC) at 112.7 °C. The substrate specificity of the nitrilase is narrow and it does not accept aromatic nitriles. The nitrilase converts the dinitriles fumaronitrile and malononitrile to their corresponding mononitriles [58],... 

Mueller, P, Egorova, K., Vorgias, C.E. et al. (2006) Cloning, overexpression, and characterization of a thermoactive nitrilase from the hyperthermophilic archaeon Pyrococcus abyssi. Protein Expression and Purification, 47, 672-668. 

Kakuta, Y., Tahara, M., Maetani, S., Yao, M., Tanaka, I., and Kimura, M. (2004). Crystal structure of the regulatory subunit of archaeal initiation factor 2B (aIF2B) from hyper-thermophilic archaeon Pyrococcus horikoshii OT3 A proposed structure of the regulatory subcomplex of eukaryotic IF2B. Biochem. Biophys. Res. Commun. 319, 725—732. 

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. ... 

FIGURE 13.2 An EPR-monitored redox titration of an Fe-O-Fe cluster with three stable oxidation states. The dinuclear iron center (= +210 mV and = +50 mV) in Pyrococcus furio-sus ferritin was titrated in the presence of a mediator mix. The fit is based on Equation 13.14. (Data from Tatur and Hagen 2005.)... 

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... 

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