Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium

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Abstract
Dormant spores of B. megaterium contained .apprx. 850 pmol of CoA/mg of dry wt. Of this total, < 1.5% was acetyl-CoA, 25% was CoA-disulfide, 43% was in disulfide linkage to protein and the remainder was the free thiol. Dormant spores of B. cereus and Clostridium bifermentans contained 700 and 600 pmol of CoA/mg of dry wt, respectively; in both species .apprx. 45% of the CoA was in disulfide linkage to protein. During germination of spores of all 3 spp., > 75% of the CoA-protein disulfides were cleaved. In B. megaterium, cleavage of these disulfides during spore germination did not require exogenous metabolites and occurred at about the same time as the initiation of germination. Much of the CoA was converted to acetyl-CoA at this time. Dormant spores also contained NADH-dependent CoA-disulfide reductase at levels higher than those in other stages of growth. The level of total CoA in growing cells was 2- to 3-fold higher than in spores. This level remained constant throughout growth and sporulation, but < 2% of the total cellular CoA was in disulfide linkage to protein until late in sporulation. The CoA-protein disulfides accumulated exclusively within the developing spore at about the time when dipicolinic acid was accumulated.

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