Open AccessFumarate reductase is a soluble enzyme in anaerobically grown Shewanella putrefaciens MR‐1
Author(s) -
Myers Charles R.,
Myers Judith M.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05483.x
Subject(s) - fumarate reductase , shewanella putrefaciens , reductase , spheroplast , lysozyme , biochemistry , periplasmic space , shewanella , enzyme , lysis , succinate dehydrogenase , cell wall , biology , chemistry , bacteria , escherichia coli , genetics , gene
The expression and distribution of fumarate reductase activity was examined in Shewanella putrefaciens MR‐1. Fumarate reductase was expressed at very low levels in aerobically grown cell and was markedly induced by growth under anaerobic conditions. Cells were fractionated into soluble and purified membrane components by four different methods. For all four methods used, and in marked contrast to the membrane‐bound fumarate reductases of other bacteria, ≧ 98% of the fumarate reductase activity was localized in the soluble fraction. In cells subjected to osmotic shock or treated with lysozyme and EDTA to form spheroplasts, the specific activity of fumarate reductase was highest in the periplasmic fraction, while the majority of total fumarate reductase activity was in the cytoplasmic fraction.