Rubredoxin from Pyrococcus furiosus

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. 2. HX results as a function of guanidinium chloride denaturant (GdmCl) for rubredoxin from Pyrococcus furiosus. Data were obtained by ID NMR at 60° and computed using Eq. (3). The results distinguish HX that occurs by local fluctuations, a subglobal unfolding, and the highest free energy global unfolding. Reprinted with permission from R. Hiller, Z. H. Zhou, M. W. W. Adams, and S. W. Englander, Proc. Natl Acad. Sci. U.S.A. 94,11329 (1997).

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]. 

The canonical rubredoxin has been purified from only one hyperthermophile, the archaeon Pyrococcus furiosus The other sequences of hyperthermophilic rubredoxins shown in Fig. 1 are putative proteins derived from genome sequences. Note that while all rubredoxins are highly similar, the hyperthermophilic... 

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