Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved γ-Proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione

Biochemistry

Volumn 49, Issue 37, 2010, Pages 8187-8196

  Hong, Baoyu ^a   Nauss, Rachel ^a   Harwood, Ian M ^a   Miller, Susan M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FLUORESCENCE; MERCURY COMPOUNDS; RATE CONSTANTS; TOXIC MATERIALS;

ARCHAEA; BROAD SPECTRUM; CATALYTIC CORE; CELLULAR THIOLS; CYTOSOLS; DIRECT MEASUREMENT; DIRECT TRANSFER; GLUTATHIONES; INTRINSIC TRYPTOPHAN FLUORESCENCES; N-TERMINAL DOMAINS; ORGANOMERCURIALS; PROTEOBACTERIA; RELATIVE EFFICIENCY; SECOND-ORDER RATE CONSTANTS; TERMINAL CYSTEINE; TOXIC EFFECT; TRYPTOPHAN FLUORESCENCE;

MERCURY (METAL);

CARBOXY TERMINAL TELOPEPTIDE; CYSTEINE; ENZYME; GLUTATHIONE; MERCURY; MERCURY (II) REDUCTASE; ORGANOMERCURIAL LYASE; ORGANOMERCURY COMPOUND; TRYPTOPHAN; UNCLASSIFIED DRUG; ALKYLMERCURY LYASE; ION; LYASE; MERCURIC REDUCTASE; METALLOCHAPERONE; OXIDOREDUCTASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DEGRADATION KINETICS; FLUORESCENCE ANALYSIS; GAMMAPROTEOBACTERIA; MEASUREMENT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; BACTERIA; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECTS; ENZYME ACTIVE SITE; FLUORESCENCE; KINETICS; METABOLISM; MOLECULAR GENETICS;

GAMMAPROTEOBACTERIA; PROTEOBACTERIA;

BACTERIA; CATALYTIC DOMAIN; CYSTEINE; FLUORESCENCE; GAMMAPROTEOBACTERIA; GLUTATHIONE; IONS; KINETICS; LYASES; MERCURY; METALLOCHAPERONES; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; TRYPTOPHAN;

EID: 77956565971     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100802k     Document Type: Article

References (39)

1. Morel, F. M. M., Kraepiel, A. M. L., and Amyot, M. (1998) The chemical cycle and bioaccumulation of mercury Annu. Rev. Ecol. Syst. 29, 543-566
2. Clarkson, T. W. and Magos, L. (2006) The toxicology of mercury and its chemical compounds Crit. Rev. Toxicol. 36, 609-662
3. Casas, J. S. and Jones, M. M. (1980) Mercury(II) complexes with sulfhydryl containing chelating agents: stability constant inconsistencies and their resolution J. Inorg. Nucl. Chem. 42, 99-102
4. 3 complexes and Hg(II)-thiol ligand exchange kinetics J. Am. Chem. Soc. 110, 6359-6364
5. Zalups, R. K. and Ahmad, S. (2005) Handling of cysteine S-conjugates of methylmercury in MDCK cells expressing human OAT1 Kidney Int. 68, 1684-1699
6. Zalups, R. K., Aslamkhan, A. G., and Ahmad, S. (2004) Human organic anion transporter 1 mediates cellular uptake of cysteine-S conjugates of inorganic mercury Kidney Int. 66, 251-261
7. Barkay, T., Miller, S. M., and Summers, A. O. (2003) Bacterial mercury resistance from atoms to ecosystems FEMS Microbiol. Rev. 27, 355-384
8. Brown, N. L. (1985) Bacterial resistance to mercury - reductio ad absurbdum? Trends Biochem. Sci. 10, 400-403
9. Banci, L., Bertini, I., Cantini, F., Massagni, C., Migliardi, M., and Rosato, A. (2009) An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1 J. Biol. Chem. 284, 9354-9360
10. + to transmembrane transport sites Proc. Natl. Acad. Sci. U.S.A. 105, 5992-5997
11. Huffman, D. L. and OHalloran, T. V. (2001) Function, structure, and mechanism of intracellular copper trafficking proteins Annu. Rev. Biochem. 70, 677-701
12. a values of the metal binding cysteine thiols (submitted).
13. 2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions Biochemistry 44, 11402-11416
14. Ledwidge, R., Soinski, R., and Miller, S. M. (2005) Direct monitoring of metal ion transfer between two trafficking proteins J. Am. Chem. Soc. 127, 10842-10843
15. Rossy, E., Seneque, O., Lascoux, D., Lemaire, D., Crouzy, S., Delangle, P., and Coves, J. (2004) Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase? FEBS Lett. 575, 86-90
16. Schue, M., Glendinning, K. J., Hobman, J. L., and Brown, N. L. (2008) Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn 501 mer operon Biometals 21, 107-116
17. Schottel, J. L. (1978) The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli J. Biol. Chem. 253, 4341-4349
18. Benison, G. C., Di Lello, P., Shokes, J. E., Cosper, N. J., Scott, R. A., Legault, P., and Omichinski, J. G. (2004) A stable mercury-containing complex of the organomercurial lyase MerB: catalysis, product release, and direct transfer to MerA Biochemistry 43, 8333-8345
19. Rossy, E., Champier, L., Bersch, B., Brutscher, B., Blackledge, M., and Coves, J. (2004) Biophysical characterization of the MerP-like amino-terminal extension of the mercuric reductase from Ralstonia metallidurans CH34 J. Biol. Inorg. Chem. 9, 49-58
20. Griffin, H. G., Foster, T. J., Silver, S., and Misra, T. K. (1987) Cloning and DNA sequence of the mercuric- and organomercurial-resistance determinants of plasmid pDU1358 Proc. Natl. Acad. Sci. U.S.A. 84, 3112-3116
21. Begley, T. P., Walts, A. E., and Walsh, C. T. (1986) Mechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial organomercurial lyase Biochemistry 25, 7192-7200
22. Begley, T. P., Walts, A. E., and Walsh, C. T. (1986) Bacterial organomercurial lyase: overproduction, isolation, and characterization Biochemistry 25, 7186-7192
23. Di Lello, P., Benison, G. C., Valafar, H., Pitts, K. E., Summers, A. O., Legault, P., and Omichinski, J. G. (2004) NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system Biochemistry 43, 8322-8332
24. Lafrance-Vanasse, J., Lefebvre, M., Di Lello, P., Sygusch, J., and Omichinski, J. G. (2008) Crystal structure of the organomercurial lyase MerB in its free and mercury-bound form: insights into the mechanism of methylmercury degradation J. Biol. Chem. 284, 938-944
25. Pitts, K. E. and Summers, A. O. (2002) The roles of thiols in the bacterial organomercurial lyase (MerB) Biochemistry 41, 10287-10296
26. Fox, B. and Walsh, C. T. (1982) Mercuric reductase-purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide J. Biol. Chem. 257, 2498-2503
27. Miller, S. M., Moore, M. J., Massey, V., Williams, C. H., Jr., Distefano, M. D., Ballou, D. P., and Walsh, C. T. (1989) Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase Biochemistry 28, 1194-1205
28. Bevington, P. R. (1969) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York.
29. Strickland, S., Palmer, G., and Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data J. Biol. Chem. 250, 4048-4052
30. Schottel, J., Mandal, A., Clark, D., Silver, S., and Hedges, R. W. (1974) Volatilisation of mercury and organomercurials determined by inducible R-factor systems in enteric bacteria Nature 251, 335-337
31. Ogawa, H. I., Tolle, C. L., and Summers, A. O. (1984) Physical and genetic map of the organomercury resistance (Omr) and inorganic mercury resistance (Hgr) loci of the IncM plasmid R831b Gene 32, 311-320
32. Momany, C., Summers, A. O., Cagle, C., and Teske, J. PDB ID 3FN8 (unpublished data).
33. Summers, A. O. (1986) Organization, expression, and evolution of genes for mercury resistance Annu. Rev. Microbiol. 40, 607-634
34. Brown, N. L., Ford, S. J., Pridmore, R. D., and Fritzinger, D. C. (1983) Nucleotide sequence of a gene from the Pseudomonas transposon Tn 501 encoding mercuric reductase Biochemistry 22, 4089-4095
35. 2 into the active site of mercuric ion reductase depend on the nature of the X ligands Biochemistry 38, 3519-3529
36. Masip, L., Veeravalli, K., and Georgiou, G. (2006) The many faces of glutathione in bacteria Antioxid. Redox Signal. 8, 753-762
37. 2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria Biochem. Pharmacol. 45, 2017-2024
38. Sedlmeier, R. and Altenbuchner, J. (1992) Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans Mol. Gen. Genet. 236, 76-85
39. Newton, G. L., Arnold, K., Price, M. S., Sherrill, C., Delcardayre, S. B., Aharonowitz, Y., Cohen, G., Davies, J., Fahey, R. C., and Davis, C. (1996) Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes J. Bacteriol. 178, 1990-1995