Chromatium

Fig. 2. H NMR spectra of (A) oxidized spinach Fe2S2 ferredoxin (33) (B) reduced spinach Fe2S2 ferredoxin (5f) (C) oxidized Desulfovibrio gigas Fe3S4 ferredoxin (138) (D) oxidized ectothiorhodospira halophila HiPIP iso-II (23) (E) reduced Chromatium vinosum HiPIP (14) (F) fully reduced Clostridium pasteurianum 2(Fe4S4) ferredoxin (139). Chemical shift values are in ppm.

The heterogeneous character of the EPR spectra given by some HIPIP is probably due to the heterogeneous location of the mixed-valence pair in the [4Fe-4S] centers, which was established in detailed NMR studies (121, 122). Since a heterogeneous location of the mixed-valence pair was also observed in the case of the [4Fe-4S] centers of Chromatium vinosum ferredoxin (123), the same phenomenon may account for the complex EPR spectra displayed by these centers in some proteins (124-126). 

The spin-lattice relaxation rate of Chromatium vinosum HIPIP was measured between 5 and 50 K (103). In comparison with the [4Fe-4S] cluster of B. stearothermophilus ferredoxin, the relaxation was found to be faster below 15 K and slower above this temperature. 

D-Arabinose occurs in arabinogalactans and arabinomannans elaborated by Mycobacterium species. When this had been determined, for example, for some arabinomannans, it was found to be furanosidic and a-linked. The arabinogalactan from Mycobacterium tuberculosis,however, contains both a- and y -linked D-arabinofuranosyl residues. It also occurs in the a-form in the LPS from Pseudomonas maltophila strain NCIB 9204. l-Arabinose is a component of the LPS from the purple, sulfur bacterium Chromatium vinosum. °... 

NiFe]-hydrogenase and models State D, Chromatium vinosum 4.2 0.05-0.15 [314]... 

While the oxidation reduction potential of the ferredoxins is —0.2 V to —0.4 V and that of the rubredoxins is about —0.05 V, a protein from the photosynthetic bacterium Chromatium has a redox potential of +0.35 V. This is the high potential iron protein, or HIPIP. 

Type III-PHA synthase is represented by the enzyme of Chromatium vino-sum and is encoded by phaECCv. It consists of the two different subunits PhaCCv and PhaECv exhibiting molecular weights of 39,730 and 40,525 Da, respectively [23]. The native PHA synthase, as isolated from recombinant strains of E. coli, exhibited a molecular weight of approximately 390 and 400 + 20 kDa as revealed in our laboratory [54] or 360 + 50 kDa but also 520 + 50 kDa as revealed in another laboratory [55]. The lower molecular weights for the holoenzyme are... 

Chromatium vinosum D Thiocystis violaceae 2311 Thiocapsa pfennigii 9111 Synechocystis sp. PCC6803... 

The polymerization behavior of hydroxybutyryl CoA by purified recombinant PHA synthase from Chromatium vinosum was different with that of Alcaligenes eutrophus [118]. This enzyme lost its activity during the polymerization and the yield and molecular weight were lower than those of Alcaligenes eutrophus. The molecular weight did not depend on the feed ratio of the monomer and enzyme. 

Rate constants for the oxidation of the negatively charge high potential Fe/S protein from Chromatium Vinosum with PCu(II) do not exhibit any dependence on pH 5.0 - 8.5 which suggests that the His 87 site is being used in this case. 

Figure 6.4 Absorption spectrum (A) and CD spectrum (B) of the [Fe4S4] cluster of a high-potential iron protein (HiPIP) from Chromatium sp. (From Cowan, 1997. Reproduced with permission from John Wiley Sons., Inc.)...

High-potential protein from Chromatium vinosum (Fe3+/Fe2+) 0.11... 

A number of publications in recent years have demonstrated an active interest in the theoretical aspects of electron transfer (ET) processes in biological systems (1.-9). This interest was stimulated by the extensive experimental information regarding the temperature dependence of ET rates measured over a broad range of temperatures (10-16). The unimolecular rate of cyto-chrome-c oxidation in Chromatium (10-12), for example, exhibits the Arrhenius type dependence and changes by three orders of... 

The temperature dependence of ET rates between cytochrome-c and the reaction center in Chromatium (Figure 1), fitted to eqs 3-5 (8), demonstrated that, unlike many redox reactions in... 

Figure 25 X-Ray structure of the active sites of the 4Fe proteins (a) HiPIP Chromatium vinosum (b) Bacillus thermoproteolyticus...

Energy supplied by sunlight is necessary for photosynthesis (Fig. 2). The fixed organic carbon is then used to generate energy via respiration. Examples of microorganisms on/in solid phases which carry out photosynthesis are Rhodospirillum, Chromatium, and Chlorobium [36,41,42,46,49,50]. 

Fig. 6. View of the Fe4S4 and a5Ru(His42) centers in Chromatium vinosum HIPIP. The edge-edge distance is 7.9 A [38]...

---