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PMID: 7035433 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Salmonella typhimurium mutants defective in the formate dehydrogenase linked to nitrate reductase.

Journal of bacteriology ·Vol. 149 ·No. 2 ·1982-02-00 ·Pages 554-60

Barrett EL, Riggs DL

Abstract

Six fdn mutants of Salmonella typhimurium defective in the formation of nitrate reductase-linked formate dehydrogenase (FDHN) but capable of producing both the hydrogenase-linked formate dehydrogenase (FDHH) and nitrate reductase were characterized. Results of phage P22 transduction experiments indicated that there may be three fdn genes located on the metE-metB chromosomal segment and distinct from all previously identified fdh and chl loci. All six FDHH+ FDHN- mutants were found to make FDHN enzyme protein which was indistinguishable from that of the wild type in electrophoretic studies. However, the results of the spectral studies indicated that all six mutants were defective in the anaerobic cytochrome b559 associated with FDHN. All contained the cytochrome b559 associated with nitrate reductase in amounts equal to or greater than the wild type. The results of the transduction experiments also indicated that the metE- metB segment of the Salmonella chromosome resembles that of Escherichia coli more than was originally thought.

MeSH Terms
Aldehyde Oxidoreductases/metabolism Ascorbic Acid/metabolism Chromosome Mapping Chromosomes, Bacterial Cytochrome b Group Cytochromes/metabolism Formate Dehydrogenases/genetics,metabolism Mutation Nitrate Reductases/metabolism Photosystem II Protein Complex Salmonella typhimurium/enzymology,genetics
Chemicals
Cytochrome b Group Cytochromes Photosystem II Protein Complex cytochrome b559 Formate Dehydrogenases Aldehyde Oxidoreductases Nitrate Reductases Ascorbic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Barrett E L
Riggs D L
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25 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1982-02-00
Pages
554-60
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC216542
Subset
IM
Grants
NIAID NIH HHS · AI-15144 · United States
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