Pyrococcus furiosus protein

For the V44A mutant of RdCp, E° shifts by more than -1-50 mV while the complementary mutation A44V in the Pyrococcus furiosus protein produces a similar but negative shift." The atom of Ala 44 in V44A of RdCp lies very close to the position of the atom of Val 44 in the native Rd (Figure 4). But the... 

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. 

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]. 

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. 

Some aspects of the proposed Rbr/Rbo oxidative stress defense system in D. vulgaris resemble those recently suggested for oxidative stress protection in the anaerobic hyperthermophilic archaeon Pyrococcus furiosus (Jenney et al. 1999). Pyrococcus furiosus contains an Nlr-like protein with superoxide reductase activity as well as an Rbr, the genes for which are tandemly located. The microorganismic segregation of SOD/catalase between aerobes and anaerobes appears to be less distinct than for Rbo/Rbr, which, as noted above, have so far been found only in air-sensitive microbes (Kirschvink et al. 2000). The latter segregation suggests that the Rbo/Rbr oxidative stress protection system is well suited to protection of anaerobic life in an aerobic world. 

In an inter-laboratoiy comparison of PMF based on MALDI-MS and PSA based on LC-MS-MS, a total of 162 2D-GE-separated protein spots from Methanococcus jannaschii and Pyrococcus furiosus were studied [35]. PSA matched 100% of the gel spots, and PMF 97%. Multiple proteins were detected in 9% and 50% of the gel spots by PMF and PSA, respectively. PSA provided better sequence coverage than PMF. 

Robust voltammetry and in situ STM to molecular resolution have been achieved when the Au(lll)-electrode surfaces are modified by linker molecules, Fig. 8-10, prior to protein adsorption. Comprehensive voltammetric data are available for horse heart cyt and P. aeruginosa The latter protein, which we address in the next Section, has in a sense emerged as a paradigm for nanoscale bioelectrochemistry. We address first briefly two other proteins, viz. the electron transfer iron-sulfur protein Pyrococcus furiosus ferredoxin and the redox metalloenz5mie Achromobacter xylosoxidans copper nitrite reductase. 

A recent detailed characterization of the putative CoADR enzyme from Pyrococcus furiosus have shown that this protein is in fact a CoA-dependent NAD(P)H elemental sulfur oxidoreductase (NSR), which is mainly involved in the reduction of S° to H2S in this heterotrophic hyperthermophile. Previous studies of the... 

Cyclic green fluorescent protein produced in vivo using an artificially split Pl-Pful intein from Pyrococcus furiosus,/. Biol. Chem. 2001, 276, 16548-16554. 

Telser, J., R. Davydov, C.-H. Kim, M.W.W. Adams, and B.M. Hoffman (1999). Investigation of the unusual electronic structure of Pyrococcus furiosus 4Fe ferredoxin by EPR spectroscopy of protein reduced at ambient and cryogenic temperatures. Inorg. Chem. 38, 3550-3553. 

Fujishima, K., Komasa, M., Kitamura, S., Suzuki, H., Tomita, M., Kanai, A. Proteome-wide prediction of novel DNA/RNA-binding proteins using amino acid composition and periodicity in the hyperther-mophilic Archaeon Pyrococcus furiosus. DNA Res. 2007,14,91-102. 

Argonne Protein Mapping Group http //www.anl.gov/ BIO/PMG/ Argonne National Laboratory, Center for Mechanistic Biology and Biotechnology, University of Chicago 2DE proteome database of Mouse liver, human breast cell lines, and Pyrococcus furiosus Free access via the internet... 

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