Summary: Glutamate induced the synthesis of 2-oxoglutarate dehydrogenase 50-fold during anaerobic growth of and, in the absence of glutamate, this enzyme was even more active in cultures sparged with N/CO (95:5, v/v). Enzyme synthesis was partially repressed when the inlet gas was passed through heated copper but totally repressed when the inlet gas was passed through alkaline pyrogallol and reduced benzyl viologen (a treatment which would remove CO as well as O). Fumarate hydratase activity also decreased but alcohol dehydrogenase and the sum of the succinate dehydrogenase and fumarate reductase activities increased when residual O was removed from the sparging gas. Soluble cytochromes and were detected in rigorously anaerobic cultures. Thus traces of O which contaminate commercial compressed N are sufficient to induce 2-oxoglutarate dehydrogenase synthesis and to affect significantly the synthesis and incorporation of respiratory chain components into the cytoplasmic membrane.


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