Germinating seedlings of mung bean (Phaseolus vulgaris L. cv. K-16) were treated with different concentrations of cadmium acetate (10, 50 and 100 μM). Cd2+ lowered the chlorophyll and heme levels. The level of lipid peroxides were higher on day 3 than on day 6. However, Cd2+ treatment significantly enhanced the level of lipid peroxides. Similarly, a dose-dependent induction of lipoxygenase (EC 1.13.11.12) activity was observed with Cd2+ treatment. Further, the activities of antioxidant enzymes such as superoxide dismutase (EC 1.15.1.1) and catalase (EC 1.11.1.6) were decreased. Our results suggest that lipoxygenase-mediated accumulation of lipid peroxides on the one hand and inhibition of free radical scavenging enzymes like superoxide dismutase and catalase on the other caused a pronounced reduction in the chlorophyll and heme levels of the seedlings. The experiments conducted on the effect of Cd2+ on dark-grown seedlings did not conform with the result of light-grown seedlings. Though chlorophyll and heme levels decreased in a dose-dependent manner, no accumulation of lipid peroxides was observed, suggesting that the inhibition of chlorophyll synthesis by Cd2+ is achieved both by reaction with constituent biosynthetic enzymes as well as peroxide-mediated degradation.

Phytotoxicity of cadmium ions on germinating seedlings of mung bean (Phaseolus vulgaris): Involvement of lipid peroxides in chlorphyll degradation

https://science.sciencemag.org/content/sci/168/3933/789.full.pdf

Enzymes Activated by Monovalent Cations

Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent.

Clostridium thermoaceticum ferments xylose, fructose, and glucose with acetate as the only product. In fermentations with mixtures of the sugars, xylose is first fermented, then fructose, and last, glucose. Fructose inhibits the fermentation of glucose, and this inhibition appears to be due to a repression of the synthesis of an enzyme needed for glucose utilization. Addition of metals to the culture medium increases the cell yield drastically from about 7 to 18 g per liter, and Y(glucose) values between 40 and 50 are obtained. According to the postulated pathways of the fermentation of glucose and synthesis of acetate from CO(2) by C. thermoaceticum, 3 mol of ATP are available as energy for growth. Thus a Y(adenosine 5'-triphosphate) of 13 to 16 is obtained. Because the normal Y(ATP) value is 10.5, this could mean that an additional source of ATP is available by an unknown mechanism. The addition of metals also increases the nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase activity, the overall reaction ((14)CO(2) --> acetate), and the incorporation of the methyl group of 5-methyltetrahydrofolate into acetate. These reactions are catalyzed very efficiently by cells harvested in early growth, whereas cells obtained at the end of a fermentation have very low formate dehydrogenase activity and capacity to incorporate CO(2) into acetate. The following enzymes involved in the synthesis of acetate from CO(2) and in the metabolism of pyruvate are present in extracts of C. thermoaceticum: 10-formyltetrahydrofolate synthetase, 5,10-methenyltetrahydrofolate cyclohydrolase, 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate reductase, phosphate acetyltransferase, and acetate kinase. These enzymes are not or are very little affected by the addition of metals to the growth medium. The amount of corrinoids in cells from early growth is low, whereas it is high in cells harvested late in growth. The opposite is found for the activity of delta-aminolevulinate dehydratase, which is high at the beginning of growth and low at the end.

Fermentation of glucose, fructose, and xylose by Clostridium thermoaceticum: effect of metals on growth yield, enzymes, and the synthesis of acetate from CO 2

D. L. Nandi

Papers

δ-Aminolevulinic Acid Dehydratase of Rhodopseudomonas spheroides: III. Mechanism of Porphobilinogen Synthesis

δ-Aminolevulinic Acid Dehydratase of Rhodopseudomonas spheroides I. ISOLATION AND PROPERTIES

δ-Aminolevulinic Acid Dehydratase of Rhodopseudomonas spheroides: II. Association to Polymers and Dissociation to Subunits