Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase

FEMS Microbiology Letters

Volumn 228, Issue 2, 2003, Pages 273-279

  Watts, Carys A ^a   Ridley, Helen ^a   Condie, Kathryn L ^a   Leaver, James T ^a   Richardson, David J ^b   Butler, Clive S ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Activity; Membrane bound enzyme; Molybdenum; Nitrate reductase; Selenate reductase; Tungsten

Indexed keywords

BENZYLVIOLOGEN; MEMBRANE ENZYME; MOLYBDATE SODIUM; MOLYBDENUM; NITRATE REDUCTASE; PARAQUAT; SELENATE; SELENITE; TUNGSTEN DERIVATIVE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CATALYSIS; CELL GROWTH; CELL MEMBRANE; ELECTRON; ENTEROBACTER CLOACAE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MEMBRANE PERMEABILITY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; REDUCTION;

ENTEROBACTER; ENTEROBACTER CLOACAE;

EID: 0344585331     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00782-1     Document Type: Article

References (23)

1. Haygarth, P.M. (1994) Global importance and global cycling of selenium. In: Selenium in the Environment (Frankenberger Jr., W.T. and Benson, S., Eds.), pp. 1-28. Marcel Dekker, New York.
2. Rayman, M. (2002) Se brought to Earth. In: Chemistry in Britain, October, pp. 28-31.
3. Stadtman T.C. Selenocysteine. Annu. Rev. Biochem. 65:1996;83-100.
4. Sabaty M., Avazeri C., Pignol D., Verméglio A. Characterization of the reduction of selenate and tellurite by nitrate reductases. Appl. Environ. Microbiol. 67:2001;5122-5126.
5. Avazeri C., Turner R.J., Pommier J., Weiner J.H., Giordano G., Verméglio A. Tellurite reductase activity of the nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite. Microbiology. 143:1997;1181-1189.
6. 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. 43:1993;135-142.
7. Schröder I., Rech S., Krafft T., Macy J.M. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272:1997;23765-23768.
8. Stolz J.F., Oremland R.S. Bacterial respiration of arsenic and selenium. FEMS Microbiol. Rev. 23:1999;615-627.
9. Krafft T., Bowen A., Theis F., Macy J.M. Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase for Thauera selenatis. DNA Seq. 10:2000;365-377.
10. Oremland R.S., Switzer Blum J., Burns Bindi A., Dowdle P.R., Herbel M., Stolz J.F. Simultaneous reduction of nitrate and selenate by cell suspensions of selenium-respiring bacteria. Appl. Environ. Microbiol. 65:1999;4385-4392.
11. Craske A., Ferguson S.J. The respiratory nitrate reductase from Paracoccus denitrificans. Molecular characterisation and kinetic properties. Eur. J. Biochem. 158:1986;429-436.
12. Losi M.E., Frankenberger W.T. Reduction of selenium oxyanions by Enterobacter cloacae SLD1a-1: isolation and growth of the bacterium and its expulsion of selenium particles. Appl. Environ. Microbiol. 63:1997;3079-3084.
13. Wolf-Watz H., Normark S., Bloom G.D. Rapid method for the isolation of large quantities of outer membrane from Escherichia coli K-12 and its application to the study of envelope mutants. J. Bacteriol. 115:1973;1191-1197.
14. Focht, D.D. (1994) Microbiological procedures for biodegradation research. In: Methods of Soil Analysis, Part 2. Microbiological and Biochemical Properties. Soil. Sci. Soc. Am. Ser. 5, pp. 407-426.
15. Dungan R.S., Frankenberger W.T. Biotransformation of selenium by Enterobacter cloacae SLD1a-1: Formation of dimethylselenide. Biogeochemistry. 55:2001;73-86.
16. Gates A.J., Hughes R.O., Sharp S.R., Millington P.D., Nilavongse A., Cole J.A., Leach E.-R., Jepson B., Richardson D.J., Butler C.S. Properties of the periplasmic nitrate reductases from Paracoccus pantotrophus and Escherichia coli after growth in tungsten-supplemented media. FEMS Microbiol. Lett. 220:2003;261-269.
17. Bell L.C., Richardson D.J., Ferguson S.J. Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyses the first step in aerobic denitrification. FEBS Lett. 265:1990;85-87.
18. Oremland R.S., Steinberg N.A., Presser T.S., Miller L.G. In situ bacterial selenate reduction in the agricultural drainage systems of western Nevada. Appl. Environ. Microbiol. 57:1991;615-617.
19. Morpeth F., Boxer D.H. Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12. Biochemistry. 24:1985;40-46.
20. Bébien M., Kirsch J., Méjean V., Verméglio A. Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli. Microbiology. 148:2002;3865-3872.
21. Taylor M.A., Jackson J.B. Threshold dependence of bacterial growth on the proton motive force. FEBS Lett. 192:1985;199-203.
22. DeMoll-Decker H., Macy J.M. The periplasmic nitrite reductase of Thauera selenatis may catalyse the reduction of selenite to elemental selenium. Arch. Microbiol. 160:1993;241-247.
23. Potter L., Angove H., Richardson D., Cole J. Nitrate reduction in the periplasm of Gram-negative bacteria. Adv. Microbial. Physiol. 45:2001;51-112.