Results 101 to 110 of about 1,210 (138)

Alternative Forms of Triosephosphate Dehydrogenase in Chromatium

Science, 1965
Triosephosphate dehydrogenase was purified extensively from the obligately phototrophic bacterium Chromatium . Enzyme prepared from photolithotrophically grown cells differed in several properties from enzyme prepared from photoorganotrophically grown cells. Either form of the enzyme could be transformed in vitro to
G A, Hudock, D B, Mellin, R C, Fuller
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Crystalline ferredoxin from the photosynthetic bacterium chromatium

Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1966
Abstract Ferredoxin has been isolated and crystallized from the photosynthetic bacterium Chromatium . It is similar to other ferredoxins in having an equivalent amount of iron and inorganic sulfide, a strongly electronegative oxidative-reduction potential and a capacity to substitute for native chloroplast ferredoxin in mediating the reduction of ...
R, Bachofen, D I, Arnon
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Light-induced electron transport in Chromatium strain D II. Light-induced absorbance changes in Chromatium chromatophores

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1968
Abstract The light-particle preparations, described previously as derived from chromatophore fractions of Chromatium, exhibit absorbance changes on steady-state illumination with actinic light. Conditions for optimal absorbance changes were established and used to study the effects of variation in redox potential effective at the light-activated ...
M A, Cusanovich, R G, Bartsch, M D, Kamen   +2 more
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Isolation of Two Hydrogenase Activities in Chromatium

European Journal of Biochemistry, 1981
Kinetic, chromatographic and electrophoretic studies of Chromatium hydrogenase show the existence in vitro of two different activities (I and II). The two hydrogenases exhibit different kinetic parameters and properties. Using reduced methyl viologen, Km and [S]0.5 values of about 20 μM and 360 μM were calculated for the hydrogenases I and II ...
M J, Llama, J L, Serra, K K, Rao, D O, Hall   +3 more
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Structural and catalytic properties of hydrogenase from Chromatium

Biochemistry, 1975
The enzyme hydrogenase, from the photosynthetic bacterium Chromatium, was purified to homogeneity after solubilization of the particulate enzyme with deoxycholate. The purification procedure included ammonium sulfate fractionation, treatment with manganous phosphate gel, heating at 63 degrees, DEAE-cellulose chromatography, and isoelectric focusing ...
P H, Gitlitz, A I, Krasna
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Evidence for three photochemical systems in Chromatium D

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1968
Abstract 1. The action spectra for oxidation of cytochrome c553, cytochrome cc′ and cytochrome c555 ★ in Chromatium D were studied. 2. Light intensity dependency of the photoinduced oxidation of the hemoproteins was studied, using light having wavelengths of 813, 853 and 904 nm as actinic light. 3. In summing up the results of the experiments, 810
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Chromatium cytochrome

Archives of Biochemistry and Biophysics, 1955
M D, KAMEN, J W, NEWTON
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Survival of Chromatium vinosum at low light intensities

Archives of Microbiology, 1980
The effect of low irradiation on the viability of Chromatium vinosum was investigated. Cultures were precultivated at 1,000 lux (μ=0.1/h). Then, before the substrate was depleted, illumination was changed to either complete darkness or about 30 lux. Previously, the latter light intensity had been found not to promote growth.
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Aerobic metabolism of Chromatium sp. strain D

Archiv f�r Mikrobiologie, 1967
1. The substrate-dependent oxygen uptake of Chromatium D has been measured. Although the rates observed were only of the order of 1 μmole/hour x mg dry weight, they are comparable with the rates found for other photosynthetic bacteria. 2. Light inhibits the rate of O2 consumption of suspensions equilibrated with excess substrate, but may
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Active transport in the photosynthetic bacterium Chromatium vinosum

Archives of Biochemistry and Biophysics, 1978
Abstract Whole cells of Chromatium vinosum show energy-dependent uptake of several amino and organic acids. The energy for metabolite uptake can be provided by light, via cyclic electron flow, or by ATP hydrolysis catalyzed by a N,N′ -dicyclohexylcarbodiimide-sensitive ATPase.
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