Structural properties of metal-free apometallothioneins

Biochemical and Biophysical Research Communications

Volumn 425, Issue 2, 2012, Pages 485-492

  Summers, Kelly L ^a   Mahrok, Anjanpreet K ^a   Dryden, Michael D M ^a   Stillman, Martin J ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

Apometallothionein; Electrospray ionization mass spectrometry; Molecular dynamics; Parabenzoquinone; Protein folding; Protein structure; Zinc metallothionein

Indexed keywords

BENZOQUINONE; CYSTEINE; METALLOPROTEIN; METALLOTHIONEIN; THIONEIN; UNCLASSIFIED DRUG; ZINC METALLOTHIONEIN;

ARTICLE; ELECTROSPRAY MASS SPECTROMETRY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING;

BENZOQUINONES; CYSTEINE; HYDROGEN-ION CONCENTRATION; METALLOTHIONEIN; METALS; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 84865392953     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.07.141     Document Type: Article

References (36)

1. Margoshes M., Vallee B.L. A cadmium protein from equine kidney cortex. J. Am. Chem. Soc. 1957, 79:4813.
2. Winge D.R., Nielson K.B. Formation of the metal-thiolate clusters of rat liver metallothionein. Environ. Health Perspect. 1984, 54:129-133.
3. Sutherland D.E.K., Stillman M.J. Noncooperative cadmium(II) binding to human metallothionein 1a. Biochem. Biophys. Res. Commun. 2008, 372:840-844.
4. Jensen L.T., Peltier J.M., Winge D.R. Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry. J. Biol. Inorg. Chem. 1998, 3:627-631.
5. Zelazowski A.J., Stillman M.J. Silver binding to rabbit liver zinc metallothionein and zinc alpha and beta fragments. Formation of silver metallothionein with silver(I):protein ratios of 6, 12, and 18 observed using circular dichroism spectroscopy. Inorg. Chem. 1992, 31:3363-3370.
6. Saito S., Kurasaki M. Gold replacement of cadmium, zinc-binding metallothionein. Res. Commun. Mol. Pathol. Pharmacol. 1996, 93:101-107.
7. Funk A.E., Day F.A., Brady F.O. Displacement of zinc from metallothionein by cadmium and by mercury. Fed. Proc. 1983, 42. 1897-1897.
8. Suzuki K.T., Maitani T. Metal-dependent properties of metallothionein-replacement invitro of zinc in zinc-thionein with copper. Biochem. J. 1981, 199:289-295.
9. Rigby K.E., Stillman M.J. Structural studies of metal-free metallothionein. Biochem. Biophys. Res. Commun. 2004, 325:1271-1278.
10. Rigby K.E., Chan J., Mackie J., Stillman M.J. Molecular dynamics study on the folding and metallation of the individual domains of metallothionein. Proteins 2006, 62:159-172.
11. Duncan K.E.R., Ngu T.T., Chan J., Salgado M.T., Merrifield M.E., Stillman M.J. Peptide folding, metal-binding mechanisms, and binding site structures in metallothioneins. Exp. Biol. Med. 2006, 231:1488-1499.
12. Duncan K.E.R., Stillman M.J. Metal-dependent protein folding: metallation of metallothionein. J. Inorg. Biochem. 2006, 100:2101-2107.
13. Chan J., Huang Z., Watt I., Kille P., Stillman M.J. Characterization of the conformational changes in recombinant human metallothioneins using ESI-MS and molecular modeling. Can. J. Chem. 2007, 85:898-912.
14. Merrifield M.E., Huang Z., Kille P., Stillman M.J. Copper speciation in the α and β domains of recombinant human metallothionein by electrospray ionization mass spectrometry. J. Inorg. Biochem. 2002, 88:153-172.
15. Chan J., Huang Z., Merrifield M.E., Salgado M.T., Stillman M.J. Studies of metal binding reactions in metallothionein by spectroscopic, molecular biology, and molecular modeling techniques. Coord. Chem. Rev. 2002, 233-234:319-339.
16. Snell J.M., Weissberger A. The reaction of thiol compounds with quinones. J. Am. Chem. 1939, 61:450-453.
17. Messerle B.A., Schaffer A., Vasak M., Kagi J.H., Wuthrich K. Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. J. Mol. Biol. 1992, 225:433-443.
18. Robbins A.H., McRee D.E., Williamson M., Collett S.A., Xuong N.H., Furey W.F., Wang B.C., Stout C.D. Refined crystal structure of Cd, Zn metallothionein at 2.0å resolution. J. Mol. Biol. 1991, 221:1269-1293.
19. Otvos J.D., Armitage I.M. Structure of the metal clusters in rabbit liver metallothionein. Proc. Natl. Acad. Sci. USA 1980, 77:7094-7098.
20. Braun W., Vasak M., Robbins A.H., Stout C.D., Wagner G., Kagi J.H., Wuthrich K. Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2. Proc. Natl. Acad. Sci. USA 1992, 89:10124-10128.
21. 18-MT formed from rabbit liver metallothionein 2. J. Am. Chem. Soc. 1994, 116:11004-11013.
22. Gui Z., Green A.R., Kasrai M., Bancroft G.M., Stillman M.J. Sulfur K-Edge EXAFS studies of cadmium-, zinc-, copper-, and silver-rabbit liver metallothioneins. Inorg. Chem. 1996, 35:6520-6529.
23. Chan J., Merrifield M.E., Soldatov A.V., Stillman M.J. XAFS spectral analysis of the cadmium coordination geometry in cadmium thiolate clusters in metallothionein. Inorg. Chem. 2005, 44:4923-4933.
24. Presta A., Fowle D.A., Stillman M.J. Structural model of rabbit liver copper metallothionein. J. Chem. Soc. Dalton Trans. 1997, 977-984.
25. Presta A., Green A.R., Zelazowski A., Stillman M.J. Copper-binding to rabbit liver metallothionein-formation of a continuum of copper(I)-thiolate stoichiometric species. Eur. J. Biochem. 1995, 227:226-240.
26. Stillman M.J. Metallothioneins. Coord. Chem. Rev. 1995, 144:461-511.
27. Grandori R. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry. J. Mass Spectrom. 2003, 38:11-15.
28. Testa L., Brocca S., Grandori R. Charge-surface correlation in electrospray ionization of folded and unfolded proteins. Anal. Chem. 2011, 83:6459-6463.
29. Peschke M., Verkerk U.H., Kebarle P. Prediction of the charge states of folded proteins in electrospray ionization. Eur. J. Mass Spectrom. 2004, 10:993-1002.
30. Kebarle P. A brief overview of the present status of the mechanisms involved in electrospray mass spectrometry. J. Mass Spectrom. 2000, 35:804-817.
31. Blindauer C.A., Polfer N.C., Keiper S.E., Harrison M.D., Robinson N.J., Langridge-Smith P.R.R., Sadler P.J. Inert site in a protein zinc cluster: isotope exchange by high resolution mass spectrometry. J. Am. Chem. Soc. 2003, 125:3226-3227.
32. Acampora G., Hermans J. Reversible denaturation of sperm whale myoglobin. Dependence on temperature, pH, and composition. J. Am. Chem. 1967, 89:1543-1547.
33. Chan J., Huang Z., Watt I., Kille P., Stillman M.J. Metallobiological necklaces: mass spectrometric and molecular modeling studying of metallation in concatenated domains of metallothionein. Chem. Eur. J. 2008, 14:7579-7593.
34. D.E.K. Sutherland, K.L. Summers, M.J. Stillman, Noncooperative metalation of metallothionein 1a and its isolated domains with zinc, Biochemistry (2012), http://dx.doi.org/10.1021/bi3004523.
35. M.F. Sanner, NIH calculator, The Scripps Research Institute, La Jolla, California, 1996. http://mgl.scripps.edu/people/sanner/html/msms_man.html.
36. Ngu T.T., Easton A., Stillman M.J. Kinetic analysis of arsenic - Metalation of human metallothionein: Significance of the two-domain structure. J. Am. Chem. Soc. 2008, 130:17016-17028.