Chromatium vinosum

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]... 

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. 

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

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

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

Allochromatium vinosum A. vinosum formerly Chromatium vinosum... 

Bagley, K. A., Van Garderen, C. J., Chen, M., Duin, E. C., Albracht, S. P. and Woodruff, W. H. (1994) Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry, 33, 9229-36. 

Davidson, G., Choudhury, S. B., Gu, Z., Bose, K., Roseboom, W., Albracht, S. P. and Maroney, M. J. (2000) Structural examination of the nickel site in chromatium vinosum hydrogenase Redox state oscillations and structural changes accompanying reductive activation and CO binding. Biochemistry, 39, 7468-79. 

Gessner, C., Stein, M., Albracht, S. P. and Lubitz, W. (1999) Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized ready state. /. Biol. Inorg. Chem., 4, 379-89. 

Happe, R. P., Roseboom, W. and Albracht, S. P. (1999) Pre-steady-state kinetics of the reactions of [NiFe]-hydrogenase from Chromatium vinosum with H2 and CO. Eur. J. Biochem., 259, 602-8. 

Van der Zwaan, J. W., Albracht, S. R, Fontijn, R. D. and Slater, E. C. (1985) Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen. FEES Lett., 179, 271-7. 

Bagley KA, Duin EC, RoseboomW, et al. 1995. Infrared-detectable groups sense changes in charge density on the nickel site in hydrogenase from Chromatium vinosum. Biochemistry 34 5527-35. 

Pershad HR, Duff JL, Heering HA, et al. 1999. Catalytic electron transport in Chromatium vinosum [NlFe]-hydrogenase application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H7H2 value. Biochemistry 38 8992-9. 

Surerus KK, Chen M, van der Zwaan JW, et al. 1994. Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mossbauer and mnltifreqnency EPR study. Biochemistry 33 4980-93. 

Van der Zwaan JW, Albracht SPJ, Fontijn RD, Roelofs YBM. 1986. EPR evidence for direct interaction of carbon monoxide with nickel in hydrogenase from Chromatium vinosum. Biochim Biophys Acta 872 208-15. 

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