Matches in SemOpenAlex for { <https://semopenalex.org/work/W1483995801> ?p ?o ?g. }
- W1483995801 endingPage "201e" @default.
- W1483995801 startingPage "147" @default.
- W1483995801 abstract "Over the last two decades, the biochemistry and genetics of dimethylsulfoxide (DMSO) and trimethylamine-N-oxide (TMAO) respiration has been characterised, particularly in Escherichia coli marine bacteria of the genus Shewanella and the purple phototrophic bacteria, Rhodobacter sphaeroides and R. capsulatus. All of the enzymes (or catalytic subunits) involved the final step in DMSO and TMAO respiration contain a pterin molybdenum cofactor and are members of the DMSO reductase family of molybdoenzymes. In E. coli, the dimethylsulfoxide reductase (DmsABC) can be purified from membranes as a complex, which exhibits quinol-DMSO oxidoreductase activity. The enzyme is anchored to the membrane via the DmsC subunit and its catalytic subunit DmsA is now considered to face the periplasm. Electron transfer to DmsA involves the DmsB subunit, which is a polyferredoxin related to subunits found in other molybdoenzymes such as nitrate reductase and formate dehydrogenase. A characteristic of the DmsAB-type DMSO reductase is its ability to reduce a variety of S- and N-oxides. E. coli contains a trimethylamine-N-oxide reductase (TorA) that is highly specific for N-oxides. This enzyme is located in the periplasm and is connected to the quinone pool via a membrane-bound penta-haem cytochrome (TorC). DorCA in purple phototrophic bacteria of the genus Rhodobacter is very similar to TorCA with the critical difference that DorA catalyses reduction of both DMSO and TMAO. It is known as a DMSO reductase because the S-oxide is the best substrate. Crystal structures of DorA and TorA have revealed critical differences at the Mo active site that may explain the differences between substrate specificity between the two enzymes. DmsA, TorA and DorA possess a twin arginine N-terminal signal sequence consistent with their secretion via the TAT secretory system and not the Sec system. The enzymes are secreted with their bound prosthetic groups: this take place in the cytoplasm and the biogenesis involves a chaperone protein, which is cognate for each enzyme. Expression of the DMSO and TMAO respiratory operons is induced in response to a fall in oxygen tension. dmsABC expression is positively controlled by the oxygen-responsive transcription factor, Fnr and ModE, a transcription factor that binds molybdate. In contrast, torCAD expression is not under Fnr- or ModE-control but is dependent upon a sensor histidine kinase-response regulator pair, TorSR, which activate gene expression under conditions of low oxygen tension in the presence of N- or S-oxide. Regulation of dorCDA expression is similar to that seen for torCAD but it appears that the expression of the sensor histidine kinase-response regulator pair, DorSR is regulated by Fnr and there is an additional tier of regulation involving the ModE-homologue MopB, molybdate and the transcription factor DorX. Analysis of microbial genomes has revealed the presence of dms and tor operons in a wide variety of bacteria and in some archaea and duplicate dms and tor operons have been identified in E. coli. Challenges ahead will include the determination of the significance of the presence of the dms operon in bacterial pathogens and the determination of the significance of DMSO respiration in the global turnover of marine organo-sulfur compounds." @default.
- W1483995801 created "2016-06-24" @default.
- W1483995801 creator A5044956761 @default.
- W1483995801 creator A5045982335 @default.
- W1483995801 creator A5058794433 @default.
- W1483995801 date "2005-01-01" @default.
- W1483995801 modified "2023-10-14" @default.
- W1483995801 title "Microbial Dimethylsulfoxide and Trimethylamine-N-Oxide Respiration" @default.
- W1483995801 cites W126841054 @default.
- W1483995801 cites W128603962 @default.
- W1483995801 cites W1481599369 @default.
- W1483995801 cites W1483663613 @default.
- W1483995801 cites W1486280561 @default.
- W1483995801 cites W1492157200 @default.
- W1483995801 cites W1499996775 @default.
- W1483995801 cites W1529114963 @default.
- W1483995801 cites W1546001194 @default.
- W1483995801 cites W1581174065 @default.
- W1483995801 cites W1590734147 @default.
- W1483995801 cites W1765467576 @default.
- W1483995801 cites W1776254535 @default.
- W1483995801 cites W1805856073 @default.
- W1483995801 cites W1813254586 @default.
- W1483995801 cites W1834248255 @default.
- W1483995801 cites W1847075919 @default.
- W1483995801 cites W1851503055 @default.
- W1483995801 cites W1928482455 @default.
- W1483995801 cites W1930087944 @default.
- W1483995801 cites W1935692179 @default.
- W1483995801 cites W1944421915 @default.
- W1483995801 cites W1948247811 @default.
- W1483995801 cites W1954489329 @default.
- W1483995801 cites W1965216692 @default.
- W1483995801 cites W1965429849 @default.
- W1483995801 cites W1966082253 @default.
- W1483995801 cites W1967250942 @default.
- W1483995801 cites W1967267586 @default.
- W1483995801 cites W1969298331 @default.
- W1483995801 cites W1969838739 @default.
- W1483995801 cites W1971084209 @default.
- W1483995801 cites W1972101693 @default.
- W1483995801 cites W1972334471 @default.
- W1483995801 cites W1972904210 @default.
- W1483995801 cites W1977416745 @default.
- W1483995801 cites W1979651924 @default.
- W1483995801 cites W197993986 @default.
- W1483995801 cites W1982254235 @default.
- W1483995801 cites W1983232006 @default.
- W1483995801 cites W1983409324 @default.
- W1483995801 cites W1983572566 @default.
- W1483995801 cites W1986582989 @default.
- W1483995801 cites W1987483478 @default.
- W1483995801 cites W1987604802 @default.
- W1483995801 cites W1988369449 @default.
- W1483995801 cites W1988741957 @default.
- W1483995801 cites W1988874660 @default.
- W1483995801 cites W1989048284 @default.
- W1483995801 cites W1989809910 @default.
- W1483995801 cites W1990595232 @default.
- W1483995801 cites W1991591611 @default.
- W1483995801 cites W1991753746 @default.
- W1483995801 cites W1992965914 @default.
- W1483995801 cites W1993321575 @default.
- W1483995801 cites W1996688710 @default.
- W1483995801 cites W1997831228 @default.
- W1483995801 cites W1998770390 @default.
- W1483995801 cites W1998967175 @default.
- W1483995801 cites W1999273752 @default.
- W1483995801 cites W2000333675 @default.
- W1483995801 cites W2000483782 @default.
- W1483995801 cites W2002327889 @default.
- W1483995801 cites W2002471123 @default.
- W1483995801 cites W2003086473 @default.
- W1483995801 cites W2003303447 @default.
- W1483995801 cites W2005488999 @default.
- W1483995801 cites W2005654635 @default.
- W1483995801 cites W2006175108 @default.
- W1483995801 cites W2008013448 @default.
- W1483995801 cites W2010816372 @default.
- W1483995801 cites W2011138732 @default.
- W1483995801 cites W2011420278 @default.
- W1483995801 cites W2012116691 @default.
- W1483995801 cites W2012786674 @default.
- W1483995801 cites W2015646183 @default.
- W1483995801 cites W2016698572 @default.
- W1483995801 cites W2018728059 @default.
- W1483995801 cites W2019170778 @default.
- W1483995801 cites W2024413424 @default.
- W1483995801 cites W2026814322 @default.
- W1483995801 cites W2026913869 @default.
- W1483995801 cites W2028090101 @default.
- W1483995801 cites W2029198060 @default.
- W1483995801 cites W2029358256 @default.
- W1483995801 cites W2030821116 @default.
- W1483995801 cites W2031215741 @default.
- W1483995801 cites W2031815017 @default.
- W1483995801 cites W2032620544 @default.
- W1483995801 cites W2032903535 @default.