Online citations, reference lists, and bibliographies.
← Back to Search

Dimethyl Sulfoxide Reductase Activity By Anaerobically Grown Escherichia Coli HB101.

P. T. Bilous, J. Weiner
Published 1985 · Biology, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
Escherichia coli grew anaerobically on a minimal medium with glycerol as the carbon and energy source and dimethyl sulfoxide (DMSO) as the terminal electron acceptor. DMSO reductase activity, measured with an artificial electron donor (reduced benzyl viologen), was preferentially associated with the membrane fraction (77 +/- 10% total cellular activity). A Km for DMSO reduction of 170 +/- 60 microM was determined for the membrane-bound activity. Methyl viologen, reduced flavin mononucleotide, and reduced flavin adenine dinucleotide also served as electron donors for DMSO reduction. Methionine sulfoxide, a DMSO analog, could substitute for DMSO in both the growth medium and in the benzyl viologen assay. DMSO reductase activity was present in cells grown anaerobically on DMSO but was repressed by the presence of nitrate or by aerobic growth. Anaerobic growth on DMSO coinduced nitrate, fumarate, and and trimethylamine-N-oxide reductase activities. The requirement of a molybdenum cofactor for DMSO reduction was suggested by the inhibition of growth and a 60% reduction in DMSO reductase activity in the presence of 10 mM sodium tungstate. Furthermore, chlorate-resistant mutants chlA, chlB, chlE, and chlG were unable to grow anaerobically on DMSO. DMSO reduction appears to be under the control of the fnr gene.



This paper is referenced by
10.1007/BF02092029
Reduction of N-oxides and sulfoxide by the same terminal reductase inProteus mirabilis
Adeline Valentine-Serano (2005)
10.1111/J.1574-6968.1991.TB04408.X
Membrane-bound respiratory system of Enterobacter cloacae strain HO1 grown anaerobically with chromate.
P. C. Wang (1991)
10.1128/JB.182.20.5779-5786.2000
The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli.
S. Gon (2000)
10.1016/j.resmic.2011.04.008
The photosynthetic membrane proteome of Rhodobacter sphaeroides R-26.1 exposed to cobalt.
F. Italiano (2011)
10.1093/emboj/17.13.3640
Overlapping functions of components of a bacterial Sec‐independent protein export pathway
F. Sargent (1998)
10.1016/J.PROCBIO.2007.07.013
Optimal dimethyl sulfoxide biodegradation using activated sludge from a chemical plant
Sz-Chwun John Hwang (2007)
10.1099/13500872-142-11-3231
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase.
J. L. Simala-Grant (1996)
10.3402/TELLUSB.V41I2.15065
Production and release of dimethyl sulfide from the Great Lakes
J. Nriagu (1989)
10.1021/BI00488A030
Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli.
R. Cammack (1990)
10.1002/ETC.5620160502
Inhibitory effects of 2‐mercaptobenzothiazole on microbial growth in a variety of trophic conditions
H. D. Wever (1997)
10.1074/jbc.M408876200
Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase*
L. Loschi (2004)
10.1111/J.1574-6968.1991.TB04473.X
Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli.
R. Daruwala (1991)
10.1074/jbc.M110.213306
Correct Assembly of Iron-Sulfur Cluster FS0 into Escherichia coli Dimethyl Sulfoxide Reductase (DmsABC) Is a Prerequisite for Molybdenum Cofactor Insertion*
Huipo Tang (2011)
10.1007/BF02012642
Microbial transformations of methylated sulfur compounds in anoxic salt marsh sediments
R. Kiene (2005)
10.1007/s10295-014-1480-x
Respiratory glycerol metabolism of Actinobacillus succinogenes 130Z for succinate production
B. Schindler (2014)
Dimethyl Sulfoxide Reductase ofEscherichia coli: anInvestigation ofFunction andAssembly byUseofInVivoComplementation
D. Sambasivarao (1991)
10.1128/JB.177.8.2057-2063.1995
Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation.
R. Rothery (1995)
10.1111/J.1574-6968.1988.TB02738.X
How is nitrogenase regulated by oxygen?
S. Hill (1988)
Participação de genes associados ao processo de respiração anaeróbica na infecção de aves por Salmonella Typhimurium
Sierra Arguello (2008)
10.1016/j.chemosphere.2010.07.001
Biological treatment of thin-film transistor liquid crystal display (TFT-LCD) wastewater using aerobic and anoxic/oxic sequencing batch reactors.
Chin-Nan Lei (2010)
10.1186/1471-2180-2-13
Oxygen and nitrate-dependent regulation of dmsABC operon expression in Escherichia coli: sites for Fnr and NarL protein interactions
S. Bearson (2002)
10.1007/978-1-4684-7612-5_9
Organic Sulfur Compounds in the Environment Biogeochemistry, Microbiology, and Ecological Aspects
D. P. Kelly (1990)
10.1016/0022-2836(91)90185-9
Bacterial DNA supercoiling and [ATP]/[ADP]. Changes associated with a transition to anaerobic growth.
L. Hsieh (1991)
10.1016/S0065-2911(05)50004-3
Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration.
Sharon L McCrindle (2005)
10.1111/j.1365-2958.1995.tb02287.x
The biogenesis of c‐type cytochromes in Escherichia coli requires a membrane‐bound protein, DipZ, with a protein disulphide isomerase‐like domain
H. Crooke (1995)
10.2323/JGAM.35.253
REDUCTION OF N-OXIDE AND S-OXIDE COMPOUNDS BY ESCHERICHIA COLI
I. Yamamoto (1989)
10.1007/BF02089418
Anaerobic induction of trimethylamine N-oxide reductase and cytochromes by dimethyl sulfoxide inEscherichia coli
I. Yamamoto (2005)
10.1080/05384680.1996.11904075
Microbial cycling of organosulfur gases in marine and freshwater environments
R. Kiene (1996)
EFFECT OF THE for MUTATION IN ESCHERICHIA ON THE TRIMETHYLAMINE N-OXIDE , NITRATE AND DIMETHYLSULFOXIDE REDUCTASES , THE FORMATE DEHYDROGENASES N AND H AND NITRATE REPRESSION COLI
I. Yamamoto (2006)
10.1016/0304-4173(85)90008-4
Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli.
S. Cole (1985)
10.1128/AEM.67.1.100-109.2001
Microbial Activity in Aquatic Environments Measured by Dimethyl Sulfoxide Reduction and Intercomparison with Commonly Used Methods
C. Griebler (2001)
10.1016/S0092-8674(00)81149-6
A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins
J. Weiner (1998)
See more
Semantic Scholar Logo Some data provided by SemanticScholar