Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli

Biochimica et Biophysica Acta - Biomembranes

Volumn 1660, Issue 1-2, 2004, Pages 66-74

  Geijer, Paulina ^a,b   Weiner, Joel H ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b LUND UNIVERSITY   (Sweden)

Author keywords

Anaerobic respiration; Dimethylsulfoxide; Membrane protein; Menaquinol; Molybdopterin guanine dinucleotide; Quinol binding

Indexed keywords

2 HEPTYL 4 HYDROXOQUINOLINE N OXIDE; ARGININE; ASPARTIC ACID; BACTERIAL ENZYME; DIMER; DIMETHYL SULFOXIDE REDUCTASE; GLUTAMATE 87; GLUTAMIC ACID; GLUTAMINE; LAPACHOL; LEUCINE; LYSINE; MENAQUINOL; PHENYLALANINE; QUINOLINE DERIVATIVE; SERINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; BACTERIAL MEMBRANE; BINDING SITE; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

EID: 1642575113     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2003.10.016     Document Type: Article

References (33)

1. Weiner J.H., Rothery R.A., Sambasivarao D., Trieber C. Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli. Biochim. Biophys. Acta. 1102:1992;1-18.
2. Bilous P.T., Weiner J.H. Molecular cloning and expression of the Escherichia coli DMSO reductase operon. J. Bacteriol. 170:1988;1511-1518.
3. Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H. Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase of Escherichia coli. Mol. Microbiol. 2:1988;785-795.
4. Simala Grant J.L., Weiner J.H. Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase. Microbiology. 142:1996;3231-3239.
5. Bilous P.T., Weiner J.H. Dimethyl sulfoxide reductase activity by anaerobically grown Escherichia coli HB101. J. Bacteriol. 162:1985;1151-1155.
6. Rothery R.A., Simala Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H. Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation. J. Bacteriol. 177:1995;2057-2063.
7. Cammack R., Weiner J.H. Electron paramagnetic resonance spectroscopic characterization of DMSO reductase of Escherichia coli. Biochemistry. 29:1990;8410-8416.
8. Rothery R.A., Weiner J.H. Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase. Biochemistry. 35:1996;3247-3257.
9. Zhao Z., Weiner J.H. Interaction of 2-n-heptyl-4-hydroxyquinoline-N- oxide with dimethyl sulfoxide reductases of Escherichia coli. J. Biol. Chem. 273:1998;20758-20763.
10. Rothery R.A., Trieber C., Weiner J.H. Interactions between the molybdenum cofactor and iron-sulfur cluster of Escherichia coli dimethylsulfoxide reductase. J. Biol. Chem. 274:1999;13002-13009.
11. Sambasivarao D., Weiner J.H. Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. J. Bacteriol. 173:1991;5935-5943.
12. Weiner J.H., Shaw G.M., Turner R.J., Trieber C. The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 268:1993;3238-3244.
13. Sambrook J., Russel D.W. Molecular Cloning: A Laboratory Manual. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
14. Rothery R.A., Weiner J.H. Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis. Biochemistry. 30:1991;8296-8305.
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
16. Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H. Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli. J. Bacteriol. 172:1990;5938-5948.
17. Jones R.W., Garland P.B. Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane. Biochem. J. 164:1977;199-211.
18. Rothery R.A., Chatterjee I., Kiema G., McDermott M.T., Weiner J.H. Hydroxylated naphtoquinones as substrates for Escherichia coli anaerobic reductases. Biochem. J. 332:1998;34-41.
19. Johnson J.L., Rajagopalan K.V. Structural and metabolic relationship between the molybdenum cofactor and urothione. Proc. Natl. Acad. Sci. U. S. A. 79:1982;6856-6860.
20. van Ark G., Berden J.A. Binding of HOQNO to beef-heart sub-mitochondrial particles. Biochim. Biophys. Acta. 459:1977;119-127.
21. Okun J.G., Lümmen P., Brandt U. Three classes of inhibition share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase). J. Biol. Chem. 274:1999;2625-2630.
22. Rich P., Fisher N. Generic features of quinone-binding sites. Biochem. Soc. Trans. 27:1999;561-565.
23. Yankovskaya V., Horsefield R., Tornroth S., Luna-Chavez C., Miyoshi H., Leger C., Byrne B., Cecchini G., Iwata S. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 299:2003;700-704.
24. Jormakka M., Tornroth S., Byrne B., Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 295:2002;1863-1868.
25. Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., Weiner J.H., Strynadka N.C.J. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10:2003;681-687.
26. Cecchini G., Schröder I., Gunsalus R.P., Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim. Biophys. Acta. 1553:2002;140-157.
27. Weiner J.H., Cammack R., Cole S.T., Condon C., Honore N., Lemire B.D., Shaw G.M. A mutant of Escherichia coli fumarate reductase decoupled from electron transport. Proc. Natl. Acad. Sci. U. S. A. 83:1986;2056-2060.
28. Westenberg D.J., Gunsalus R.P., Ackrell B.A., Cecchini G. Electron transfer from menaquinol to fumarate. Fumarate reductase anchor polypeptide mutants of Escherichia coli. J. Biol. Chem. 265:1990;19560-19567.
29. Rothery R.A., Weiner J.H. Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase. Eur. J. Biochem. 254:1998;588-595.
30. Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1961-1966.
31. Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J. Biol. Chem. 277:2002;16124- 16130.
32. Westenberg D.J., Gunsalus R.P., Ackrell B.A., Sices H., Cecchini G. Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones. J. Biol. Chem. 268:1993;815-822.
33. Lancaster C.R.D., Gross R., Haas A., Ritter M., Mantele W., Simon J., Kroger A. Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase. Proc. Natl. Acad. Sci. U. S. A. 97:2000;13051-13056.