Isolation and characterization of a transposon mutant of Shewanella putrefaciens MR-1 deficient in fumarate reductase. Lett Appl Microbiol 1997 Sep;25(3):162-8
Date
11/14/1997Pubmed ID
9351256DOI
10.1046/j.1472-765x.1997.00196.xScopus ID
2-s2.0-0030805368 (requires institutional sign-in at Scopus site) 24 CitationsAbstract
A transposon mutant, designated CMTn-3, of Shewanella putrefaciens MR-1 that was deficient in fumarate reduction was isolated and characterized. In contrast to the wild-type, CMTn-3 could not grow anaerobically with fumarate as the electron acceptor, and it lacked benzyl viologen-linked fumarate reductase activity. Consistent with this, CMTn-3 lacked a 65 kDa c-type cytochrome, which is the same size as the fumarate reductase enzyme. CMTn-3 retained the wild-type ability to use nitrate, iron(III), manganese(IV) and trimethylamine N-oxide (TMAO) as terminal electron acceptors. The results indicate that the loss of the fumarate reductase enzyme does not affect other anaerobic electron transport systems in this bacterium.
Author List
Myers CR, Myers JMMESH terms used to index this publication - Major topics in bold
Base SequenceDNA Primers
DNA Transposable Elements
Electron Transport
Fumarates
Genes, Bacterial
Gram-Negative Facultatively Anaerobic Rods
Mutagenesis, Insertional
Mutation
Subcellular Fractions
Succinate Dehydrogenase
