Isolation and characterization of a transposon mutant of Shewanella putrefaciens MR-1 deficient in fumarate reductase.
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.
Myers
C R
CR
Department of Pharmacology and Toxicology, Medical College of Wisconsin, Milwaukee 53226, USA. cmyers@post.its.mcw.edu
Myers
J M
JM
D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D004251:DNA Transposable Elements / Q000235:genetics; D004579:Electron Transport; D005650:Fumarates / Q000378:metabolism; D005798:Genes, Bacterial; D006092:Gram-Negative Facultatively Anaerobic Rods / Q000201:enzymology* / Q000235:genetics* / Q000254:growth & development; D016254:Mutagenesis, Insertional; D009154:Mutation; D013347:Subcellular Fractions / Q000201:enzymology; D013385:Succinate Dehydrogenase / Q000172:deficiency / Q000235:genetics*
D017931:DNA Primers; D004251:DNA Transposable Elements; D005650:Fumarates; C032005:fumaric acid; D013385:Succinate Dehydrogenase