Thiocapsa roseopersicina hydrogenase

N. A. Zorin, B. Dimon, J. Gagnon, J. Gaillard, P. Carrier, P. M. Vignais (1996) Inhibition by iodoacetamide and acetylene of the H-D exchange reaction catalyzed by Thiocapsa roseopersicina hydrogenase. Eur. J. Biochem., 241 675-681... 

N. A. Zorin (1986) Inhibition of Thiocapsa roseopersicina hydrogenase by various compounds. Biokhimiya. (Russ.), 51 770-774... 

Figure 2. EPR spectra from Thiocapsa roseopersicina hydrogenase obtained on samples used in XAS experiments at 77 K. The spectra are arranged in order of decreasing redox potential top to bottom. Forms A and B correspond to oxidized enzyme, SI is an EPR silent intermediate, form C is an active form of the enzyme that is also EPR-active, and R is the fully reduced enzyme. (Reproduced from reference 35. Copyright 1993 American Chemical Society.)...

Figure 14. EPR spectra o/Thiocapsa roseopersicina hydrogenase, Ni-C (top) and Ni-L (bottom). Spectra were taken at 77 K, at a microwave frequency of 9.62 GHz, a microwave power of 20 raW, and a modulation amplitude of 4 G.

Figure 15. 2H-ENDOR spectra of the solvent exchangeable protons associated with Thiocapsa roseopersicina hydrogenase in form C (A) and its photoproduct (B).

Oh Y-K, Lee Y-J, Choi E-H, Kim M-S (2008) Bioelectrocatalytic hydrogen production using Thiocapsa roseopersicina hydrogenase in two-compartment fuel cells. Int J Hydrogen Energy 33 5218-5223. doi 10.1016/j.ijhydene.2008.05.015... 

EPR spectra and g values for the various states of the hydrogenase from Thiocapsa roseopersicina 64) are depicted in Fig. 4. These spectra are representative of those of the other NiFe hydrogenases. 

K. L. Kovdcs, Cs. Bagyinka (1990) Structural properties and functional states of hydrogenase from Thiocapsa roseopersicina. FEMS Microbiol. Rev., 87 407-412... 

G. Rakhely, A. Colbeau, J. Garin, P. M. Vignais, K. L. Kovacs (1998) Unusual gene organization of HydSL, the stable [NiFe] hydrogenase in the photosynthetic bacterium Thiocapsa roseopersicina. J. Bacterial., 180 1460-1465... 

The oxidation of hydrogen in fuel cells provides clean energy and water as the only byproduct. Application of hydrogenase for hydrogen electrode is able to improve the characteristics of the fuel cells. Thermostable hydrogenase from Thiocapsa roseopersicina is an appropriate catalyst for development of several systems for production and transformation of renewable energy based on molecular hydrogen. 

S. V. Morozov, E. E. Karyakina, N. A. Zorin, S. D. Varfolomeyev, S. Cosnier, A. A. Karyakin (2002) Direct and electrically wired bioelectrocatalysis by hydrogenase from Thiocapsa roseopersicina. Bioelectrochemistry, 55 169-171... 

Dihydrogen can be rather easily evolved with Systems 10-15 of Table 1, where, with PET across the membrane, the water-soluble radical cation MV+ is produced outside the vesicle. This radical cation can evolve dihydrogen from water in the presence of various catalysts. This was demonstrated by Tsvetkov et al. [262] for System 12 of Table 1. As a catalyst, the c water soluble hydrogenase from Thiocapsa roseopersicina was used or a heterogeneous rhodium-polymer catalyst [263]. The quantum yield of H2 production was comparable with the quantum yield of MV+ generation. 

Many biomolecules feature metal ions in a mixed donor set, and the area is intensively studied. As an example, the active site of the hydrogenase from thiocapsa roseopersicina features nickel in a mixed 0,N,S donor environment. Definition of the ligand donor set in biopolymers is not always facile, however, so they tend to be overlooked as examples of mixed donor ligands. There are some small biomolecule examples extant. 

A hydrogenase isolated from a photosynthetic bacterium Thiocapsa roseopersicina strain BBS shows a profound stability against oxygen and heat (Gogotov et al., 1978 Zorin, 1986 Zorin et al., 1995). The hydrogenase is used to make a functional hydrogenase LB film since the hydrogenase (Noda et al., 1998). 

Gogotov, IN, Zorin, NA Serebriakova, LT and Kondratieva, EN. (1978). The properties of hydrogenase from the phototrophic bacterium Thiocapsa roseopersicina. Biochim. Biophys. Acta 523, 335-343. 

The hydrogen reaction involves the processes of ionization and evolution of molecular hydrogen. To achieve activation of these processes, hydrogenases from fluorotrophic bacteria Thiocapsa roseopersicina and Chloro-pseudomas ethylica have been used. 

Complementation with hypF gene from T. roseopersicina in a AhypF strain of R capsulatus was successful, a clear demonstration that a functionally active form of this Thiocapsa gene product is synthesised by the R capsulatus cells from the foreign template. The same experiment using a AhypF E. coli strain resulted in barely detectable complementation. We conclude that there must be strain dependent variations in the complementation capacity and that the most thoroughly studied bacterium, E. coli, may not be the best choice for such complementation studies of hydrogenase assembly and biosynthesis. 

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