Induction by Oxygen of Respiration and Phosphorylation of Anaerobically Grown Escherichia coli
Author(s) -
B. Z. Cavari,
Y. AviDor,
N. Grossowicz
Publication year - 1968
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.96.3.751-759.1968
Subject(s) - biology , biochemistry , respiratory chain , malate dehydrogenase , succinate dehydrogenase , oxidase test , respiration , escherichia coli , enzyme , dehydrogenase , cytochrome c oxidase , nicotinamide adenine dinucleotide phosphate , oxygen , chemistry , botany , organic chemistry , gene
The changes occurring in the respiratory enzymes of anaerobically grownEscherichia coli strain B andE. coli 15 T− A− U− bar during exposure to oxygen were studied. Reduced nicotinamide adenine dinucleotide (NADH) oxidase activity reached its peak soon after O2 exposure; cytochrome content and succinate oxidase activity increased more slowly, and these increases paralleled each other. The activities of isocitrate and malate dehydrogenases also increased, but the increase was less than that of the succinate and NADH oxidases; exposure to O2 had no effect on the succinate and NADH dehydrogenase activities. On the other hand, the glycolytic activity decreased slowly after O2 exposure. The incorporation of32 P into acid-soluble organic phosphate esters paralleled the respiratory rate during the first 60 min after O2 exposure, but continued to increase after the respiration reached a plateau. The sensitivity of32 P incorporation to the uncoupler carbonyl cyanidem -chlorophenylhydrazone also increased with time. The observed relationship between the development of the respiratory chain and the energy-conserving mechanism during O2 exposure is discussed. Synthesis of the respiratory enzymes upon exposure to oxygen was dependent on concomitant protein and ribonucleic acid synthesis but not on deoxyribonucleic acid synthesis.
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