Flavin-adenine dinucleotide and diaphorase in resting and germinated spores, and vegetative cells of Bacillus subtilis and Bacillus megatherium

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Abstract
Flavin-adenine dinucleotide was shown to be present in resting spores, germinated spores, and vegetative cells of laboratory strains of Bacillus subtilis and B. megaterium, and resting spores of B. subtilis N. C. T. C. 85. During germination of spores of the laboratory strains of B. subtilis and B. megaterium in chemically defined media, no change in total flavin-adenine dinucleotide content, or in the relative amts. of free and bound dinucleotide occurred. No L-amino-acid oxidase, D-amino-acid oxidase or xanthine oxidase activity could be demonstrated in resting spores of B. subtilis and B. megaterium or in germinated spores of B. megaterium and the laboratory strain of B. subtilis. An enzyme capable of oxidizing reduced coenzyme I and reducing methylene blue occurred in all types of cells of B. subtilis and B. megaterium. Spores of B. megaterium contained a heat-stable substance which inhibited reduction of methylene blue by heart diaphorase, the inhibition being prevented by the addition of large amts. (1 mg.) of coenzyme 1. No O2 uptake could be measured with resting spores of the laboratory B. subtilis in phosphate buffer. The QO2 of these spores in buffered glucose, after preliminary heating at 60[degree] for 15 min., was 0.42. O2 uptake of B. subtilis and B. megaterium spores increased approx. 2uo times following germination. This O2 uptake was considerably less sensitive to cyanide than that of fully developed vegetative cells.