Thermostable properties of the periplasmic selenate reductase from Thauera selenatis

Biochimie

Volumn 92, Issue 10, 2010, Pages 1268-1273

  Dridge, Elizabeth J ^a   Butler, Clive S ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

Author keywords

Molybdoenzyme; Selenate reduction; Thermo stability; Tungstoenzyme

Indexed keywords

BACTERIAL ENZYME; MOLYBDENUM; SELENATE REDUCTASE; TUNGSTEN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; BINDING AFFINITY; CELL GROWTH; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME ISOLATION; KINETICS; NONHUMAN; PH; TEMPERATURE; THAUERA; THAUERA SELENATIS; THERMOSTABILITY;

BACTERIAL PROTEINS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MOLYBDENUM; OXIDOREDUCTASES; PERIPLASM; PROTEIN BINDING; THAUERA; THERMODYNAMICS; TUNGSTEN;

ARCHAEA; THAUERA SELENATIS;

EID: 77957111715     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.06.003     Document Type: Article

References (29)

1. Martinez-Espinosa R.M., Dridge E.J., Bonete M.J., Butt J.N., Butler C.S., Sargent F., Richardson D.J. Look on the positive side! The orientation, identification and bioenergetics of ″ Archaeal″ membrane-bound nitrate reductases. FEMS Microbiol. Lett. 2007, 276:129-139.
2. Afshar S., Johnson E., De Vries S., Schröder I. Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilium. J. Bacteriol. 2001, 183:5491-5495.
3. Sargent F. Constructing the wonders of the bacterial world: biosynthesis of complex enzymes. Microbiology 2007, 153:633-651.
4. Berks B.C., Sargent F., Palmer T. The Tat protein export pathway. Mol. Microbiol. 2000, 35:260-274.
5. Johnson H.A., Pelletier D.A., Spormann A.M. Isolation and characterization of anaerobic ethylbenzene dehydrogenase, a novel Mo-Fe-S enzyme. J. Bacteriol. 2001, 183:4536-4542.
6. Kloer D.P., Hagel C., Heider J., Schulz G.E. Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum. Structure 2006, 14:1377-1388.
7. McDevitt C.A., Hanson G.R., Noble C.J., Cheesman M.R., McEwan A.G. Characterization of the redox centers in dimethyl sulfide dehydrogenase from Rhodovulum sulfidophilum. Biochemistry 2002, 41:15234-15244.
8. McDevitt C.A., Hugenholtz P., Hanson G.R., McEwan A.G. Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes. Mol. Microbiol. 2002, 44:1575-1587.
9. Schröder I., Rech S., Krafft T., Macy J.M. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 1997, 272:23765-23768.
10. Thorell H.D., Stenklo K., Karlsson J., Nilsson T. A gene cluster for chlorate metabolism in Ideonella dechloratans. Appl. Environ. Microbiol. 2003, 69:5585-5592.
11. Karlsson J., Nilsson T. The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution. Protein Expr. Purif. 2005, 41:306-312.
12. Krafft T., Bowen A., Theis F., Macy J.M. Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis. DNA Seq. 2000, 10:365-377.
13. Dridge E.J., Watts C.A., Jepson B.J.N., Line K., Santini J.M., Richardson D.J., Butler C.S. Investigation of the redox centres of selenate reductase from Thauera selenatis by electron paramagnetic resonance spectroscopy. Biochem. J. 2007, 408:19-28.
14. Dridge E.J., Richardson D.J., Lewis R.J., Butler C.S. Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus. Biochem. Soc. Trans. 2006, 34:118-121.
15. Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 2003, 10:681-687.
16. Jormakka M., Richardson D.J., Byrne B., Iwata S. The architecture of NarGH reveals a structural classification of MGD enzymes. Structure 2004, 12:95-104.
17. Lowe E.C., Bydder S., Hartshorne R.S., Tape H.L.U., Dridge E.J., Debieux C.M., Paszkiewicz K., Singleton I., Lewis R.J., Santini J.M., Richardson D.J., Butler C.S. Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis. J. Biol. Chem. 2010, 285:18433-18442.
18. Sharmasarkar S., Vance G.F. Soil and plant selenium at a reclaimed uranium mine. J. Environ. Qual. 2002, 31:1516-1521.
19. Johnson M.K., Rees D.C., Adams M.W.W. Tungstoenzymes. Chem. Rev. 1996, 96:2817-2839.
20. Afshar S., Kim C., Monbouquette H.G., Schröder I. Effect of tungstate on nitrate reduction by the hyperthermophilic archaeon Pyrobaculum aerophilium. Appl. Environ. Microbiol. 1998, 64:3004-3008.
21. Macy J.M., Rech S., Auling G., Dorsch M., Stackenbrandt E., Sly L.I. Thauera selenatis gen-nov, sp-nov, a member of the beta-subclass of proteobacteria with a novel type of anaerobic respiration. Int. J. Syst. Bacteriol. 1993, 43:135-142.
22. Craske A.L., Ferguson S.J. The respiratory nitrate reductase from Paracoccus denitrificans. Molecular characterisation and kinetic properties. Eur. J. Biochem. 1986, 158:429-436.
23. Watanabe T., Honda K. Measurement of the extinction coefficient of the methyl viologen cation radical and the efficiency of its formation by semiconductor photocatalysis. J. Phys. Chem. 1982, 86:2617-2619.
24. Ridley H., Watts C.A., Richardson D.J., Butler C.S. Development of a viologen based microtitre plate assay for the analysis of oxyanion reductase activity: application to the membrane bound selenate reductase from Enterobacter cloacae SLD1a-1. Anal. Biochem. 2006, 358:289-294.
25. Rech S.A., Macy J.M. The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes. J. Bacteriol. 1992, 174:7316-7320.
26. Buc J., Santini C.-L., Giordani R., Czjzek M., Wu L.-F., Giordano G. Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli. Mol. Microbiol. 1999, 32:159-168.
27. Wang J.-J., Tessier C., Holm R.H. Analogue reaction systems of selenate reductase. Inorg. Chem. 2006, 45:2979-2988.
28. Huber R., Sacher M., Vollmann A., Huber H., Rose D. Respiration of arsenate and selenate by hyperthermophilic archaea. Syst. Appl. Microbiol. 2000, 23:305-314.
29. Knott R., Fallick A.E., Richards K.J., Bäcker H. Mineralogical and sulphur isotope characteristics of a massive sulfide boulder, Galapagos Rift, 85-550W. Hydrothermal Vents and Processes 1995, vol. 87:207-222. Geological Society Special Publication. L.M. Parson, C.L. Walker, D.R. Dixon (Eds.).