Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection

Analytical Biochemistry

Volumn 435, Issue 1, 2013, Pages 74-82

  Sardi, Florencia ^a   Manta, Bruno ^b   Portillo Ledesma, Stephanie ^a   Knoops, Bernard ^c   Comini, Marcelo A ^b   Ferrer Sueta, Gerardo ^a  

^a UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

^b INSTITUT PASTEUR DE MONTEVIDEO   (Uruguay)

^c UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

Catalytic cysteine; Nucleophilicity; Thiol

Indexed keywords

AMINO ACIDS; CHEMICAL SENSORS; IONIZATION; MOLECULAR WEIGHT; PROTEINS;

CATALYTIC CYSTEINES; DIFFERENTIAL REACTIVITIES; HIGH THROUGHPUT SCREENING; MONOTHIOL GLUTAREDOXIN; NANOMOLAR CONCENTRATION; NUCLEOPHILICITIES; SECOND-ORDER RATE CONSTANTS; THIOL;

RATE CONSTANTS;

BROMOBIMANE; CAPTOPRIL; CYSTEINE; GLUTAREDOXIN; LOW MOLECULAR WEIGHT THIOL; PEROXIREDOXIN 5; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HIGH THROUGHPUT SCREENING; IONIZATION; NUCLEOPHILICITY; PH; PRIORITY JOURNAL; PROTEIN DETERMINATION; TRYPANOSOMA BRUCEI;

TRYPANOSOMA BRUCEI;

EID: 84873331479     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2012.12.017     Document Type: Article

References (56)

1. H.F. Gilbert Molecular and cellular aspects of thiol-disulfide exchange Adv. Enzymol. Relat. Areas Mol. Biol. 63 1990 69 172
2. G. Ferrer-Sueta, B. Manta, H. Botti, R. Radi, M. Trujillo, and A. Denicola Factors affecting protein thiol reactivity and specificity in peroxide reduction Chem. Res. Toxicol. 24 2011 434 450
3. A.C. Storer, and R. Menard Catalytic mechanism in papain family of cysteine peptidases Methods Enzymol. 244 1994 486 500
4. Z.Y. Zhang Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development Annu. Rev. Pharmacol. Toxicol. 42 2002 209 234
5. T. Linsky, and W. Fast Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily Biochim. Biophys. Acta 2010 1804 1943 1953
6. G. Roos, S. Loverix, E. Brosens, K. Van Belle, L. Wyns, P. Geerlings, and J. Messens The activation of electrophile, nucleophile, and leaving group during the reaction catalysed by pI258 arsenate reductase Chembiochem 7 2006 981 989 (Pubitemid 43938622)
7. W.A. Munroe, C.A. Lewis Jr., and R.B. Dunlap Kinetics of sulfhydryl group modification of thymidylate synthetase: a proposal for activation of catalytic cysteinly residues Biochem. Biophys. Res. Commun. 80 1978 355 360 (Pubitemid 8271879)
8. J.L. Ferrer, J.M. Jez, M.F. Bowman, R.A. Dixon, and J.P. Noel Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis Nat. Struct. Biol. 6 1999 775 784 (Pubitemid 29360240)
9. G.L. Ellman Tissue sulfhydryl groups Arch. Biochem. Biophys. 82 1959 70 77
10. C.V. Smythe The reaction of iodoacetate and of iodoacetamide with various sulfhydryl groups, with urease and with yeast preparations J. Biol. Chem. 114 1936 601 612
11. E. Friedmann, D.H. Marrian, and I. Simonreuss Mitosis of chick fibroblasts in the presence of unsaturated imides and sulphydryl compounds Biochim. Biophys. Acta 9 1952 61 64
12. L. Hellerman, F.P. Chinard, and V.R. Deitz Protein sulfhydryl groups and the reversible inactivation of the enzyme urease J. Biol. Chem. 147 1943 443 462
13. L. Moroder, H.J. Musiol, and R. Scharf Aziridine-2-carboxylic acid: a reactive amino acid unit for a new class of cysteine proteinase inhibitors FEBS Lett. 299 1992 51 53
14. 2 is not reflected in its reaction with other oxidants and thiol reagents J. Biol. Chem. 282 2007 11885 11892 (Pubitemid 47100684)
15. H.C. Hawkins, and R.B. Freedman The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase Biochem. J. 275 1991 335 339
16. G.B. Kallis, and A. Holmgren Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli J. Biol. Chem. 255 1980 10261 10265 (Pubitemid 11214607)
17. R.A. Bednar Reactivity and pH dependence of thiol conjugation to N-ethylmaleimide: detection of a conformational change in chalcone isomerase Biochemistry 29 1990 3684 3690 (Pubitemid 20142710)
18. W.P. Jencks Binding energy, specificity, and enzymic catalysis: the Circe effect Adv. Enzymol. Relat. Areas Mol. Biol. 43 1975 219 410
19. a of redox cysteines: the key role of hydrogen bonding Antioxid. Redox Signal. 18 2013 94 127
20. G.M. Whitesides, J.E. Lilburn, and R.P. Szajewski Rates of thiol-disulfide interchange reactions between mono- and dithiols and Ellman's reagent J. Org. Chem. 42 1977 332 338
21. M. Friedman, J.F. Cavins, and J.S. Wall Relative nucleophilic reactivities of amino groups and mercaptide ions in addition to reactions with α,β-unsaturated compounds J. Am. Chem. Soc. 87 1965 3672 3682
22. J.W. Nelson, and T.E. Creighton Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo Biochemistry 33 1994 5974 5983 (Pubitemid 24184604)
23. M.F. Jeng, A. Holmgren, and H.J. Dyson Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction Biochemistry 34 1995 10101 10105
24. J.D. Forman-Kay, G.M. Clore, and A.M. Gronenborn Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR Biochemistry 31 1992 3442 3452
25. D.D. Roberts, S.D. Lewis, D.P. Ballou, S.T. Olson, and J.A. Shafer Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate Biochemistry 25 1986 5595 5601
26. R.A. MacQuarrie, and S.A. Bernhard Mechanism of alkylation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenase Biochemistry 10 1971 2456 2466
27. Z.R. Gan, and W.W. Wells Identification and reactivity of the catalytic site of pig liver thioltransferase J. Biol. Chem. 262 1987 6704 6707
28. N.S. Kosower, E.M. Kosower, G.L. Newton, and H.M. Ranney Bimane fluorescent labels: labeling of normal human red cells under physiological conditions Proc. Natl. Acad. Sci. USA 76 1979 3382 3386 (Pubitemid 9233965)
29. E.M. Kosower, and N.S. Kosower Bromobimane probes for thiols Methods Enzymol. 251 1995 133 148
30. A.E. Radkowsky, and E.M. Kosower Bimanes: 17. (Haloalkyl)-1,5- diazabicyclo[3.3.O]octadienediones (halo-9,10-dioxabimanes): reactivity toward the tripeptide thiol, glutathione J. Am. Chem. Soc. 108 1986 4527 4531
31. P.B. Hulbert, and S.I. Yakubu Monobromobimane: a substrate for the fluorimetric assay of glutathione transferase J. Pharm. Pharmacol. 35 1983 384 386 (Pubitemid 13095570)
32. D.R. Grassetti, and J.F. Murray Jr. Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine Arch. Biochem. Biophys. 119 1967 41 49
33. B. Knoops, A. Clippe, C. Bogard, K. Arsalane, R. Wattiez, C. Hermans, E. Duconseille, P. Falmagne, and A. Bernard Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family J. Biol. Chem. 274 1999 30451 30458
34. J.P. Declercq, C. Evrard, A. Clippe, D.V. Stricht, A. Bernard, and B. Knoops Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution J. Mol. Biol. 311 2001 751 759 (Pubitemid 32803733)
35. M.A. Comini, J. Rettig, N. Dirdjaja, E.M. Hanschmann, C. Berndt, and R.L. Krauth-Siegel Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes J. Biol. Chem. 283 2008 27785 27798
36. M. Filser, M.A. Comini, M.M. Molina-Navarro, N. Dirdjaja, E. Herrero, and R.L. Krauth-Siegel Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1 Biol. Chem. 389 2008 21 32 (Pubitemid 350308201)
37. K.J. Ellis, and J.F. Morrison Buffers of constant ionic strength for studying pH-dependent processes Methods Enzymol. 87 1982 405 426
38. H. Kanety, and E.M. Kosower Bimanes: 15. Kinetics and mechanism of the hydroxide ion reaction with 1,5-diazabicyclo[3.3.0]octadienediones (9,10-dioxabimanes) J. Org. Chem. 47 1982 42222 44226
39. L. Hu, and R.F. Colman Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111 Biochemistry 36 1997 1635 1645
40. D.L. Rabenstein, and A.A. Isab Conformational and acid-base equilibriums of captopril in aqueous solution Anal. Chem. 54 1982 526 529 (Pubitemid 12140224)
41. W. Stricks, and I.M. Kolthoff Equilibrium constants of the reactions of sulfite with cystine and with dithiodiglycolic acid J. Am. Chem. Soc. 73 1951 4569 4574
42. R.E. Benesch, and R. Benesch The acid strength of the -SH group in cysteine and related compounds J. Am. Chem. Soc. 77 1955 5877 5881
43. S. Barelier, D. Linard, J. Pons, A. Clippe, B. Knoops, J.M. Lancelin, and I. Krimm Discovery of fragment molecules that bind the human peroxiredoxin 5 active site PLoS One 5 2010 e9744
44. C. Evrard, A. Smeets, B. Knoops, and J.-P. Declercq Crystal structure of the C47S mutant of human peroxiredoxin 5 J. Chem. Crystallogr. 34 2004 553 558 (Pubitemid 39237813)
45. A. Hall, D. Parsonage, L.B. Poole, and P.A. Karplus Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization J. Mol. Biol. 402 2010 194 209
46. M. Dubuisson, D. Vander Stricht, A. Clippe, F. Etienne, T. Nauser, R. Kissner, W.H. Koppenol, J.F. Rees, and B. Knoops Human peroxiredoxin 5 is a peroxynitrite reductase FEBS Lett. 571 2004 161 165 (Pubitemid 38992941)
47. M. Trujillo, A. Clippe, B. Manta, G. Ferrer-Sueta, A. Smeets, J.P. Declercq, B. Knoops, and R. Radi Pre-steady state kinetic characterization of human peroxiredoxin 5: taking advantage of Trp84 fluorescence increase upon oxidation Arch. Biochem. Biophys. 467 2007 95 106 (Pubitemid 47625297)
48. B. Mannervik, and K. Axelsson Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol Biochem. J. 149 1975 785 788
49. J. Melchers, N. Dirdjaja, T. Ruppert, and R.L. Krauth-Siegel Glutathionylation of trypanosomal thiol redox proteins J. Biol. Chem. 282 2007 8678 8694 (Pubitemid 47093487)
50. a values Biochemistry 19 1980 4156 4166
51. K.F. Discola, M.A. de Oliveira, J.R. Rosa Cussiol, G. Monteiro, J.A. Barcena, P. Porras, C.A. Padilla, B.G. Guimaraes, and L.E. Netto Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae J. Mol. Biol. 385 2009 889 901
52. E. Loumaye, G. Ferrer-Sueta, B. Alvarez, J.F. Rees, A. Clippe, B. Knoops, R. Radi, and M. Trujillo Kinetic studies of peroxiredoxin 6 from Arenicola marina: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide Arch. Biochem. Biophys. 514 2011 1 7
53. P. Giron, L. Dayon, and J.C. Sanchez Cysteine tagging for MS-based proteomics Mass Spectrom. Rev. 30 2011 366 395
54. E. Weerapana, C. Wang, G.M. Simon, F. Richter, S. Khare, M.B. Dillon, D.A. Bachovchin, K. Mowen, D. Baker, and B.F. Cravatt Quantitative reactivity profiling predicts functional cysteines in proteomes Nature 468 2010 790 795
55. E.M. Kosower, B. Pazhenchevski, H. Dodiuk, H. Kanety, and D. Faust Bimanes: 6. Reactive halogen derivatives of syn- and anti-1,5-diazabicyclo[3.3. 0]octadienediones (9,10-dioxabimanes) J. Org. Chem. 46 1981 1666 1673
56. B. Manta, C. Pavan, M. Sturlese, A. Medeiros, M. Crispo, C. Berndt, L. Krauth-Siegel, M. Bellanda, M.A.Comini, Iron-sulfur cluster (ISC) binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of ISC coordination and relevance for parasite infectivity, Antioxid. Redox Signal. 2013, http://dx.doi.org/10.1089/ars.2012.4859.