The Library
Dimethylsulfide is an energy source for the heterotrophic marine bacterium Sagittula stellata
Tools
Boden, Rich, Murrell, J. C. (J. Colin) and Schäfer, Hendrik. (2011) Dimethylsulfide is an energy source for the heterotrophic marine bacterium Sagittula stellata. FEMS Microbiology Letters, Vol.322 (No.2). pp. 188-193. ISSN 0378-1097
Full text not available from this repository.
Official URL: http://dx.doi.org/10.1111/j.1574-6968.2011.02349.x
Abstract
Dimethylsulfide (DMS) is a volatile organosulfur compound, ubiquitous in the oceans, that has been credited with various roles in biogeochemical cycling and in climate control. Various oceanic sinks of DMS are known - both chemical and biological - although they are poorly understood. In addition to the utilization of DMS as a carbon or a sulfur source, some Bacteria are known to oxidize it to dimethylsulfoxide (DMSO). Sagittula stellata is a heterotrophic member of the Alphaproteobacteria found in marine environments. It has been shown to oxidize DMS during heterotrophic growth on sugars, but the reasons for and the mechanisms of this oxidation have not been investigated. Here, we show that the oxidation of DMS to DMSO is coupled to ATP synthesis in S. stellata and that DMS acts as an energy source during chemoorganoheterotrophic growth of the organism on fructose and on succinate. DMS dehydrogenase (which is responsible for the oxidation of DMS to DMSO in other marine Bacteria) and DMSO reductase activities were absent from cells grown in the presence of DMS, indicating an alternative route of DMS oxidation in this organism.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
| Divisions: | Faculty of Science > Life Sciences (2010- ) |
| Library of Congress Subject Headings (LCSH): | Dimethyl sulfide, Energy metabolism, Marine microbiology, Bioenergetics, Heterotrophic bacteria |
| Journal or Publication Title: | FEMS Microbiology Letters |
| Publisher: | Wiley-Blackwell Publishing Ltd. |
| ISSN: | 0378-1097 |
| Date: | September 2011 |
| Volume: | Vol.322 |
| Number: | No.2 |
| Page Range: | pp. 188-193 |
| Identification Number: | 10.1111/j.1574-6968.2011.02349.x |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| Funder: | Natural Environment Research Council (Great Britain) (NERC) |
| Grant number: | NE/B501404/1 (NERC), NE/E013333/1 (NERC) |
| References: | Adams B, Smith AT, Bailey S, McEwan AG & Bray RC (1999) Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and with dimethyl sulfoxide: complexities revealed by conventional and stopped-flow spectrophotometry. Biochemistry 38: 8501–8511. Anthony C (1982) The Biochemistry of Methylotrophs. Academic Press, London, UK. Baumberger JP (1933) Apparatus for the study of redox potential in biological systems. J Gen Physiol 17: 1–6. Bentley R & Chasteen TG (2004) Environmental VOSCs – formation and degradation of dimethyl sulfide, methanethiol and related materials. Chemosphere 55: 291–317. Boden R, Kelly DP, Murrell JC & Sch¨afer H (2010) Oxidation of dimethylsulfide to tetrathionate by Methylophaga thiooxidans sp. nov.: a new link in the sulfur cycle. Environ Microbiol 12: 2688–2699. Boden R, Borodina E,Wood AP, Kelly DP,Murrell JC & Sch¨afer H (2011) Purification and characterization of dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans. J Bacteriol 193: 1250–1258. Borodina E, Kelly DP, Schumann P, Rainey FA, Ward-Rainey NL & Wood AP (2002) Enzymes of dimethylsulfone metabolism and the phylogenetic characterization of the facultative methylotrophs Arthrobacter sulfonivorans sp. nov., Arthrobacter methylotrophus sp. nov. and Hyphomicrobium sulfonivorans sp. nov. Arch Microbiol 177: 173–183. Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein–dye binding. Anal Chem 72: 248–254. Charlson R, Lovelock J, Andreae M & Warren S (1987) Oceanic phytoplankton, atmospheric sulphur, cloud albedo and climate. Nature 326: 655–661. del Valle DA, Kieber DJ, Bisgrove J & Kiene RP (2007) Lightstimulated production of DMSO by a particle-associated process in the Ross Sea, Antarctica. Limnol Oceanogr 52: 2456–2466. del Valle DA, Kieber DJ, Toole DA, Bisgrove J & Kiene RP (2009) Dissolved DMSO production via biological and photochemical oxidation of dissolved DMS in the Ross Sea, Antarctica. Deep-Sea Res Pt I 56: 166–177. Gonz´alez JM, Mayer F, Moran MA, Hodson RE & Whitman WB (1997) Sagittula stellata gen. nov., sp. nov., a lignintransforming bacterium from a coastal environment. Int J Syst Bacteriol 47: 773–780. Green DH, Shenoy DM, Hart MC & Hatton AC (2011) Coupling of dimethylsulfide oxidation to biomass production by a marine Flavobacterium. Appl Environ Microbiol 77: 3137–3140. Hatton AD (2002) DMSP removal and DMSO production in sedimenting particulate matter in the northern North Sea. Deep-Sea Res Pt II 49: 3053–3065. Kelly DP & Syrett PJ (1964) Inhibition of formation of adenosine triphosphate in Thiobacillus thioparus by 2:4-dinitrophenol. Nature 202: 597–598. Kelly DP & Wood AP (1994) Synthesis and determination of thiosulfate and polythionates. Methods in Enzymology 243: Inorganic Microbial Sulfur Metabolism (Peck HD Jr & LeGall J, eds), pp. 475–501. Academic Press Inc., San Diego. Li M, Yuan DX, Li QL & Jin XY (2007) Sequential analysis of dimethyl sulfur compounds in seawater. Chin Chem Lett 18: 99–102. Mason J & Kelly DP (1988) Mixotrophic and autotrophic growth of Thiobacillus thiooxidans on tetrathionate. Arch Microbiol 149: 317–323. McDevitt CA, Hugenholtz P, Hanson GR & McEwan AG (2002) Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterincontaining enzymes. Mol Microbiol 44: 1575–1587. |
| URI: | http://wrap.warwick.ac.uk/id/eprint/38515 |
Data sourced from Thomson Reuters' Web of Knowledge
Actions (login required)
![]() |
View Item |
Tools
Tools

