Effect of growth substrate on enzymes of the citric and glyoxylic acid cycles in Thiobacillus novellus.

Abstract

A quantitative study was conducted of enzymes involved in the citric acid cycle and associated systems of the facultative autotroph Thiobacillus novellus grown on five different substrates. Irrespective of the growth substrate the organism possessed complete citric and glyoxylic acid cycles and the specific activity of α-ketoglutarate dehydrogenase was always quite low. Also, the activities of the enzymes of both cycles were usually lowest in extracts from autotrophic cells, and highest in extracts from acetate-grown cells. The three remaining extracts had activities that were between the two extremes with those from glucose-grown cells generally lower than those from pyruvate and succinate. Several exceptions should be noted among these generalizations. For example, the activity of aconitate hydratase and malic dehydrogenase was lowest in extracts from glucose-grown cells while that of isocitric dehydrogenase was lowest in extracts from pyruvate-grown cells. Transhydrogenase activity was virtually absent from extracts of pyruvate- and succinate-grown cells while NADH oxidase, which was identical in these two extracts, was also relatively low. Of interest is the large amount of cytochrome c found in high-speed supernatants. In extracts from autotrophic cells this was about 2.3% of the soluble protein and is suggestive of a significant role being played by the electron-transport system during growth of the organism.