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Home / Equine Research Bank / Arch Biochem Biophys / Specific electrochemical iodination of horse heart myoglobin...
Archives of biochemistry and biophysics2008; 474(1); 1-7; doi: 10.1016/j.abb.2008.02.032

Specific electrochemical iodination of horse heart myoglobin at tyrosine 103 as determined by Fourier transform ion cyclotron resonance mass spectrometry.

Abstract: The iodination of proteins remains a useful tool in biochemistry for radiolabelling. However, chemical or enzymatic iodination is difficult to control and can give deleterious polyiodination. Previously, we have shown that electrooxidation with nitrite is a rapid method for the selective nitration of tyrosine residues in proteins. In principle, it should be possible to substitute a number of electrooxidisable anions into the tyrosine phenol ring. Electrochemical iodination is more difficult to control than nitration because the rapid anodic oxidation of I(-) leads to persistent formation of the iodinating triiodide anion. However, application of pulsed electrooxidation and reduction cycles is shown to be an effective procedure for the selective mono and double-iodination of myoglobin, which may have general application to other proteins in controlling of the level of iodination. Mono- and double-iodination of myoglobin by this method was confirmed by electrospray FT-ICR mass spectrometry. Infrared multiphoton dissociation (IRMPD) enabled localization of the site of mono-iodination to be restricted to either His97 or Tyr103. More extensive sequence coverage was obtained with electron capture dissociation (ECD), allowing unambiguous assignment of the site of iodination to Tyr103.
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Publication Date: 2008-02-29 PubMed ID: 18348862PubMed Central: PMC2568815DOI: 10.1016/j.abb.2008.02.032Google Scholar: Lookup
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  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research explores a method for specifically iodinating horse heart myoglobin at tyrosine 103. This selective iodination used pulsed electrooxidation and reduction cycles and was confirmed by mass spectrometry.

Objective of the Research

  • The study aimed at developing a more controlled process for protein iodination. This is important in biochemistry, particularly for radiolabelling purposes.

Challenge in Iodination Process

  • The traditional methods of iodination which comprise chemical or enzymatic iodination are hard to control and can result in polyiodination, which can harm the structure and function of the protein.
  • Specifically, electrochemical iodination is difficult due to the rapid anodic oxidation of I(-) leading to a persistent formation of the iodinating triiodide anion.

Proposed Solution

  • The researchers used electrooxidation with nitrite, a method they had previously found to be effective for selective nitration of tyrosine residues in proteins.
  • They proposed that this process could facilitate the substitution of several electro-oxidizable anions into the tyrosine phenol ring.
  • They applied pulsed electrooxidation and reduction cycles, providing a controlled procedure for the selective mono and double-iodination of myoglobin.

Method Confirmation and Protein Localization

  • The researchers confirmed the mono and double iodination of myoglobin using electrospray FT-ICR mass spectrometry.
  • They used Infrared Multiphoton Dissociation (IRMPD) to determine the site of mono-iodination to either His97 or Tyr103.
  • For a more detailed sequence coverage, they used electron capture dissociation (ECD). This provided a clear method to identify the site of iodination to Tyr103.

Significance of the Findings

  • The findings could be significant for the process of protein iodination. The described method offers a more controlled approach to protein iodination, which could be particularly beneficial for proteomic studies and radiolabelling applications.

Cite This Article

APA
Iniesta J, Cooper HJ, Marshall AG, Heptinstall J, Walton DJ, Peterson IR. (2008). Specific electrochemical iodination of horse heart myoglobin at tyrosine 103 as determined by Fourier transform ion cyclotron resonance mass spectrometry. Arch Biochem Biophys, 474(1), 1-7. https://doi.org/10.1016/j.abb.2008.02.032

Publication

Archives of biochemistry and biophysics
ISSN: 1096-0384
NlmUniqueID: 0372430
Country: United States
Language: English
Volume: 474
Issue: 1
Pages: 1-7

Researcher Affiliations

Iniesta, Jesus
  • Centre for Molecular and Biomedical Science, Faculty of Health and Life Sciences, Coventry University, Coventry CV1 5FB, UK.
Cooper, Helen J
    Marshall, Alan G
      Heptinstall, John
        Walton, David J
          Peterson, Ian R

            MeSH Terms

            • Animals
            • Cyclotrons
            • Electrochemistry / methods
            • Horses
            • Mass Spectrometry / methods
            • Myoglobin / chemistry
            • Spectrophotometry, Ultraviolet
            • Spectroscopy, Fourier Transform Infrared
            • Tyrosine / chemistry

            References

            This article includes 38 references
            1. Marino VJ, Sterin-Prync AE, Carbonetto CH, Roguin LP. Conformational and sequential epitopes on the human granulocyte-colony stimulating factor molecule (hG-CSF) and their role in binding to human placenta receptors.. Cytokine 2001 Oct 21;16(2):41-50.
              pubmed: 11683584doi: 10.1006/cyto.2001.0943google scholar: lookup
            2. Zhang M, Mizrachi D, Fanelli F, Segaloff DL. The formation of a salt bridge between helices 3 and 6 is responsible for the constitutive activity and lack of hormone responsiveness of the naturally occurring L457R mutation of the human lutropin receptor.. J Biol Chem 2005 Jul 15;280(28):26169-76.
              pmc: PMC1237128pubmed: 15908694doi: 10.1074/jbc.m502102200google scholar: lookup
            3. Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jörnvall H, Gutierrez R, Eyzaguirre J. Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase.. Acta Crystallogr D Biol Crystallogr 1999 Apr;55(Pt 4):779-84.
              pubmed: 10089308doi: 10.1107/s0907444999000244google scholar: lookup
            4. Collier TL, Schiller PW, Waterhouse RN. Radiosynthesis and in vivo evaluation of the pseudopeptide delta-opioid antagonist [(125)I]ITIPP(psi).. Nucl Med Biol 2001 May;28(4):375-81.
              pubmed: 11395309doi: 10.1016/s0969-8051(01)00193-7google scholar: lookup
            5. Jilaveanu LB, Zito CR, Oliver D. Dimeric SecA is essential for protein translocation.. Proc Natl Acad Sci U S A 2005 May 24;102(21):7511-6.
              pmc: PMC1140455pubmed: 15897468doi: 10.1073/pnas.0502774102google scholar: lookup
            6. Rubina K, Talovskaya E, Cherenkov V, Ivanov D, Stambolsky D, Storozhevykh T, Pinelis V, Shevelev A, Parfyonova Y, Resink T, Erne P, Tkachuk V. LDL induces intracellular signalling and cell migration via atypical LDL-binding protein T-cadherin.. Mol Cell Biochem 2005 May;273(1-2):33-41.
              pmc: PMC1282457pubmed: 16013438doi: 10.1007/s11010-005-0250-5google scholar: lookup
            7. Fraker PJ, Speck JC Jr. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril.. Biochem Biophys Res Commun 1978 Feb 28;80(4):849-57.
              pubmed: 637870doi: 10.1016/0006-291x(78)91322-0google scholar: lookup
            8. Salacinski PR, McLean C, Sykes JE, Clement-Jones VV, Lowry PJ. Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenyl glycoluril (Iodogen).. Anal Biochem 1981 Oct;117(1):136-46.
              pubmed: 7316186doi: 10.1016/0003-2697(81)90703-xgoogle scholar: lookup
            9. Walton D.J., Richards P.G., Heptinstall J., Coles B. Electrochim. Acta. 1997;42:2285–2294.
            10. Richards PG, Coles B, Heptinstall J, Walton DJ. Electrochemical modification of lysozyme: anodic reaction of tyrosine residues.. Enzyme Microb Technol 1994 Sep;16(9):795-801.
              pubmed: 7765098doi: 10.1016/0141-0229(94)90038-8google scholar: lookup
            11. Kendall G, Cooper HJ, Heptinstall J, Derrick PJ, Walton DJ, Peterson IR. Specific electrochemical nitration of horse heart myoglobin.. Arch Biochem Biophys 2001 Aug 15;392(2):169-79.
              pubmed: 11488590doi: 10.1006/abbi.2001.2451google scholar: lookup
            12. Matters D, Cooper HJ, McDonnell L, Iniesta J, Heptinstall J, Derrick P, Walton D, Peterson I. Mass spectrometry in demonstrating the site-specific nitration of hen egg white lysozyme by an improved electrochemical method.. Anal Biochem 2006 Sep 15;356(2):171-81.
              pubmed: 16899211doi: 10.1016/j.ab.2006.06.033google scholar: lookup
            13. Sokolovsky M, Riordan JF, Vallee BL. Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins.. Biochem Biophys Res Commun 1967 Apr 7;27(1):20-5.
              pubmed: 6048236doi: 10.1016/s0006-291x(67)80033-0google scholar: lookup
            14. Souza JM, Daikhin E, Yudkoff M, Raman CS, Ischiropoulos H. Factors determining the selectivity of protein tyrosine nitration.. Arch Biochem Biophys 1999 Nov 15;371(2):169-78.
              pubmed: 10545203doi: 10.1006/abbi.1999.1480google scholar: lookup
            15. Scortichini CL, Bartlett JM. Electrolytic Cell and Process for the Labeling of Proteins and Peptides. United States Patent 524656, 1993.
            16. Rosenberg RA, Muzaffar SA, Heersche JN, Jez D, Murray TM. Preparation and properties of biologically active radioiodinated parathyroid hormone.. Anal Biochem 1983 Feb 1;128(2):331-41.
              pubmed: 6846810doi: 10.1016/0003-2697(83)90383-4google scholar: lookup
            17. Sammon PJ, Brand JS, Neuman WF, Raisz LG. Metabolism of labeled parathyroid hormone. I. Preparation of biologically active I-125-labeled parathyroid hormone.. Endocrinology 1973 Jun;92(6):1596-603.
              pubmed: 4707255doi: 10.1210/endo-92-6-1596google scholar: lookup
            18. Marshall AG, Hendrickson CL, Jackson GS. Fourier transform ion cyclotron resonance mass spectrometry: a primer.. Mass Spectrom Rev 1998 Jan-Feb;17(1):1-35.
              pubmed: 9768511doi: 10.1002/(sici)1098-2787(1998)17:1<1::aid-mas1>3.0.co;2-kgoogle scholar: lookup
            19. Little DP, Speir JP, Senko MW, O'Connor PB, McLafferty FW. Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing.. Anal Chem 1994 Sep 15;66(18):2809-15.
              pubmed: 7526742doi: 10.1021/ac00090a004google scholar: lookup
            20. Cooper HJ, Håkansson K, Marshall AG. The role of electron capture dissociation in biomolecular analysis.. Mass Spectrom Rev 2005 Mar-Apr;24(2):201-22.
              pubmed: 15389856doi: 10.1002/mas.20014google scholar: lookup
            21. Senko M.W., Hendrickson C.L., Emmett M.R., Shi S.D.H., Marshall A.G. J. Am. Soc. Mass Spectrom. 1997;8:970–976.
            22. J.P. Quinn, M.R. Emmett, A.G. Marshall, in: 46th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, 1998.
            23. Beu S.C., Laude D.A. Int. J. Mass Spectrom. Ion Proc. 1992;112:215–230.
            24. Malmberg J.H., O’Neil T.M. Phys. Rev. Lett. 1977;39:1333–1336.
            25. Senko MW, Canterbury JD, Guan S, Marshall AG. A high-performance modular data system for Fourier transform ion cyclotron resonance mass spectrometry.. Rapid Commun Mass Spectrom 1996;10(14):1839-44.
              pubmed: 8953786doi: 10.1002/(sici)1097-0231(199611)10:14<1839::aid-rcm718>3.0.co;2-vgoogle scholar: lookup
            26. Shi S.D.H., Drader J.J., Freitas M.A., Hendrickson C.L., Marshall A.G. Int. J. Mass Spectrom. 2000;195:591–598.
            27. G.T. Blakney, G. van der Rest, J.R. Johnson, M. Freitas, J.J. Drader, S.D.H. Shi, C.L. Hendrickson, N.L. Kelleher, A.G. Marshall, in: 49th ASMS Conference on Mass Spectrometry and Allied Topics, Chicago, IL, 2001.
            28. Marshall A.G., Wang T.C.L., Ricca T.L. J. Am. Chem. Soc. 1985;107:7893–7897.
            29. Guan S., Marshall A.G. Int. J. Mass Spectrom. Ion Proc. 1996;158:5–37.
            30. Akkermans R.P., Qiu F.L., Roberts S.L., Suarez M.F., Compton R.G. J. Phys. Chem. B. 1999;103:8319–8327.
            31. Taylor J.E., Evans M.I. Ohio J. Sci. 1953;53:37–41.
            32. Dané L.M., Janssen L.J.J., Hoogland J.G. Electrochim. Acta. 1968;13:507–518.
            33. Swathirajan S., Bruckenstein S. J. Electroanal. Chem. 1980;25:25–38.
            34. Lund H, Hammerich O. Organic Electrochemistry. fourth ed. Marcel Dekker Inc.; 2001. p. 590.
            35. Nakanishi I, Miyazaki K, Shimada T, Iizuka Y, Inami K, Mochizuki M, Urano S, Okuda H, Ozawa T, Fukuzumi S, Ikota N, Fukuhara K. Kinetic study of the electron-transfer oxidation of the phenolate anion of a vitamin E model by molecular oxygen generating superoxide anion in an aprotic medium.. Org Biomol Chem 2003 Nov 21;1(22):4085-8.
              pubmed: 14664398doi: 10.1039/b306758kgoogle scholar: lookup
            36. Eickhoff H., Jung G., Rieker A. Tetrahedron. 2001;57:353–364.
            37. Cren-Olivé C, Hapiot P, Pinson J, Rolando C. Free radical chemistry of flavan-3-ols: determination of thermodynamic parameters and of kinetic reactivity from short (ns) to long (ms) time scale.. J Am Chem Soc 2002 Nov 27;124(47):14027-38.
              pubmed: 12440901doi: 10.1021/ja0262434google scholar: lookup
            38. Glazer A.N. In: third ed. Neurath H., Hills R.L., editors. vol. 2. Academic Press; New York: 1976. pp. 1–103. (The Proteins).

            Citations

            This article has been cited 8 times.
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