The activity of hydrogenase was assayed in the intact cells and subcellular fractions of Brevibacterium flavum. The organism was shown to have the membrane-bound form of hydrogenase. The soluble NAD+-reducing hydrogenase was not found.
View Article and Find Full Text PDFPrikl Biokhim Mikrobiol
April 1984
The growth of the culture and biosynthesis of lysin were studied in Brevibacterium flavum 22 LD cultivated in a chemostat. During cultivation the flow rate of the medium and the partial pressure of oxygen dissolved in the medium were varied. The maximum yield of lysine, calculated in respect to the sucrose consumed, (Yp = g lysine .
View Article and Find Full Text PDFA coordination was established between the rate of glucose transport and the activity of enzymes involved in glycolysis and the citric acid cycle (CAC) in Brevibacterium flavum cells producing lysine: the rate of glucose transport and the activity of enzymes catalysing glycolysis increased when the activity of CAC enzymes decreased and vice versa. The activity of glycolytic enzymes and the rate of glucose transport in the cells increased also when electron transport through the respiration chain was inhibited and when oxidation and phosphorylation in the respiration chain were uncoupled. The rate of ATP synthesis in the cells is presumed to coordinate the rate of glucose transport and the activity of glycolytic and CAC enzymes in the cells.
View Article and Find Full Text PDFThe rate of oxygen uptake (QO2) was shown to increase in the chemostat culture of a Brevibacterium flavum 22 LD auxotrophic strain at D = 0.13 h-1 after addition of chlorocarbonylcyanide phenylhydrazone. The index of respiration control reached 1.
View Article and Find Full Text PDFA scheme is proposed for the branched respiratory chain in Brevibacterium flavum 22 LD. Three branching sites in the main electron transport pathway are suggested: at the initial stage of NADH2 oxidation (before menaquinone) and at the levels of cytochromes b and c. Up to 40% out of the total oxygen is consumed in the NADH2-dependent alternative oxidative pathway in the presence of 5.
View Article and Find Full Text PDFNauchnye Doki Vyss Shkoly Biol Nauki
January 1974