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Nitrofurazone-reducing enzymes in E. coli and their role in drug activation in vivo.
Metadata
Journalcanadian journal of microbiology1.793Date
1975-Oct
Publication Type
Journal Article
Volume
1975-Oct / 21 : 1484-91
Author
McCalla DR , Olive P , Tu Y , Fan ML
DoiPMIDMESH
Aerobiosis
Anaerobiosis
Cell-Free System
DNA, Bacterial
Escherichia coli
Hot Temperature
Hydrogen-Ion Concentration
Isoenzymes
Molecular Weight
Mutation
Nitrofurazone
Nucleic Acid Denaturation
Oxidation-Reduction
Oxidoreductases
Abstract
Earlier work showed that Escherichia coli contains at least two enzymes which reduce nitrofurazone and other nitrofuran derivatives. One of these enzymes is lacking in some nitrofurazone-resistant mutant strains. We now report that there are three separable nitrofuran reductases in this organism: reductase I (mol. wt. approximately 50 000, insensitive to O2), reductase IIa (mol. wt. approximately 120 000, inhibited by oxygen), reductase IIb (mol. wt. approximately 700 000, inhibited by O2). Unstable metabolites formed during the reduction of nitrofurazone by preparations containing reductases IIa and IIb produce breaks in DNA in vitro. In vivo experiments with nitrofurazone-resistant strains, which lack reductase II but contain reductases IIa and IIb, demonstrated that lethality, mutation, and DNA breakage are all greatly increased when cultures are incubated under anaerobic conditions, i.e., conditions such that reductase II is active. These results provide further evidence for the importance of reductive activation of nitrofurazone.
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Can J Microbiolcanadian journal of microbiology
Metadata
LocationCanada
FromCANADIAN SCIENCE PUBLISHING

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