Modulation of the electrochemical behavior of tyrosyl radicals by the electrode surface

Analytical Biochemistry

Volumn 362, Issue 1, 2007, Pages 89-97

  Machczynski, Michael C ^a   Kuhl, Kendra P ^a   McGuirl, Michele A ^a  

^a UNIVERSITY OF MONTANA   (United States)

Author keywords

Azurin; Electrochemistry; Electrode; Ionization; Oxidation; Potential; Radical; Reduction; SAM; Tyrosine; Voltammetry

Indexed keywords

AMINO ACIDS; ELECTROCHEMISTRY; ELECTRODES; ENZYME ACTIVITY; ENZYME ELECTRODES; IONIZATION; IONIZATION POTENTIAL; OXIDATION; PEPTIDES; REDOX REACTIONS; REDUCTION; VOLTAMMETRY;

AZURIN; ELECTROCHEMICAL BEHAVIORS; ELECTRODE SURFACES; MODIFIED ELECTRODES; POTENTIAL; RADICAL; TYROSINE; VOLTAMMETRIC SIGNALS;

ELECTROCHEMICAL ELECTRODES;

AZURIN; CYSTEINE; GOLD; TYROSINE;

ARTICLE; COVALENT BOND; ELECTROCHEMISTRY; ELECTRODE; ENZYME ACTIVITY; IONIZATION; OXIDATION REDUCTION POTENTIAL; PKA; POTENTIOMETRY; PRIORITY JOURNAL; PROTEIN BINDING;

EID: 33846654090     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.11.040     Document Type: Article

References (54)

1. Armstrong F.A., and Wilson G.S. Recent developments in faradaic bioelechemistry. Electrochim. Acta 45 (2000) 2623-2645
2. Armstrong F.A. Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites. Curr. Opin. Chem. Biol. 9 (2005) 110-117
3. Leger C., Lederer F., Guigliarelli B., and Bertrand P. Electron flow in multicenter enzymes: theory, applications, and consequences on the natural design of redox chains. J. Am. Chem. Soc. 128 (2006) 180-187
4. Gray H.B., and Winkler J.R. Long-range electron transfer. Proc. Natl. Acad. Sci. USA 102 (2005) 3534-3539
5. Armstrong F.A., Butt J.N., and Sucheta A. Voltammetric studies of redox-active centers in metalloproteins adsorbed on electrodes. Methods Enzymol. 227 (1993) 479-500
6. Jeuken L.J., Connell S.D., Henderson P.J., Gennis R.B., Evans S.D., and Bushby R.J. Redox enzymes in tethered membranes. J. Am. Chem. Soc. 128 (2006) 1711-1716
7. Rusling J.F. Enzyme bioelectrochemistry in cast biomembrane-like films. Acc. Chem. Res. 31 (1998) 363-369
8. Frew J.E., and Hill H.A. Direct and indirect electron transfer between electrodes and redox proteins. Eur. J. Biochem. 172 (1988) 261-269
9. Armstrong F.A., Hill H.A.O., and Walton N.J. Direct electrochemistry of redox proteins. Acc. Chem. Res. 21 (1988) 407-413
10. Stubbe J., and van Der Donk W.A. Protein radicals in enzyme catalysis. Chem. Rev. 98 (1998) 705-762
11. Reece S.Y., Hodgkiss J.M., Stubbe J., and Nocera D.G. Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology. Philos. Trans. R. Soc. Lond. B Biol. Sci. 361 (2006) 1351-1364
12. Reece S.Y., Stubbe J., and Nocera D.G. pH dependence of charge transfer between tryptophan and tyrosine in dipeptides. Biochim. Biophys. Acta 1706 (2005) 232-238
13. DeFilippis M.R., Murthy C.P., Broitman F., Weinraub D., Faraggi M., and Klapper M.H. Electrochemical properties of tyrosine phenoxy and tryptophan indolyl radicals in peptides and amino acid analogues. J. Phys. Chem. 95 (1991) 3416-3419
14. DeFilippis M.R., Murthy C.P., Faraggi M., and Klapper M.H. Pulse radiolytic measurement of redox potentials: the tyrosine and tryptophan radicals. Biochemistry 28 (1989) 4847-4853
15. Harriman A. Further comments on the redox potentials of tryptophan and tyrosine. J. Phys. Chem. 91 (1987) 6102-6104
16. Jovanovic S.V., Harriman A., and Simic M.G. Electron-transfer reactions of tryptophan and tyrosine derivatives. J. Phys. Chem. 90 (1986) 1935-1939
17. Tommos C., Skalicky J.J., Pilloud D.L., Wand A.J., and Dutton P.L. De novo proteins as models of radical enzymes. Biochemistry 38 (1999) 9495-9507
18. a. Biochemistry 44 (2005) 11891-11902
19. Hess C.R., Juda G.A., Dooley D.M., Amii R.N., Hill M.G., Winkler J.R., and Gray H.B. Gold electrodes wired for coupling with the deeply buried active site of Arthrobacter globiformis amine oxidase. J. Am. Chem. Soc. 125 (2003) 7156-7157
20. Belliston-Bittner W., Dunn A.R., Nguyen Y.H., Stuehr D.J., Winkler J.R., and Gray H.B. Picosecond photoreduction of inducible nitric oxide synthase by rhenium(I)-diimine wires. J. Am. Chem. Soc. 127 (2005) 15907-15915
21. Dunn A.R., Dmochowski I.J., Winkler J.R., and Gray H.B. Nanosecond photoreduction of cytochrome P450cam by channel-specific Ru-diimine electron tunneling wires. J. Am. Chem. Soc. 125 (2003) 12450-12456
22. Farver O., and Pecht I. Blue copper proteins as a model for investigating electron transfer processes within polypeptide matrices. Biophys. Chem. 50 (1994) 203-216
23. Fujita K., Nakamura N., Ohno H., Leigh B.S., Niki K., Gray H.B., and Richards J.H. Mimicking protein-protein electron transfer: voltammetry of Pseudomonas aeruginosa azurin and the Thermus thermophilus Cu(A) domain at omega-derivatized self-assembled-monolayer gold electrodes. J. Am. Chem. Soc. 126 (2004) 13954-13961
24. Miller J.E., Di Bilio A.J., Wehbi W.A., Green M.T., Museth A.K., Richards J.R., Winkler J.R., and Gray H.B. Electron tunneling in rhenium-modified Pseudomonas aeruginosa azurins. Biochim. Biophys. Acta 1655 (2004) 59-63
25. Pascher T., Bergstrom J., Malmstrom B.G., Vanngard T., and Lundberg L.G. Modification of the electron-transfer sites of Pseudomonas aeruginosa azurin by site-directed mutagenesis. FEBS Lett. 258 (1989) 266-268
26. Pascher T., Karlsson B.G., Nordling M., Malmstrom B.G., and Vanngard T. Reduction potentials and their pH dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa. Eur. J. Biochem. 212 (1993) 289-296
27. Armstrong F.A., Barlow N.L., Burn P.L., Hoke K.R., Jeuken L.J., Shenton C., and Webster G.R. Fast, long-range electron-transfer reactions of a "blue" copper protein coupled non-covalently to an electrode through a stilbenyl thiolate monolayer. Chem. Commun. (Camb.) (2004) 316-317
28. Hirst J., and Armstrong F.A. Fast-scan cyclic voltammetry of protein films on pyrolytic graphite edge electrodes: characteristics of electron exchange. Anal. Chem. 70 (1998) 5062-5071
29. Di Bilio A.J., Crane B.R., Wehbi W.A., Kiser C.N., Abu-Omar M.M., Carlos R.M., Richards J.H., Winkler J.R., and Gray H.B. Properties of photogenerated tryptophan and tyrosyl radicals in structurally characterized proteins containing rhenium(I) tricarbonyl diimines. J. Am. Chem. Soc. 123 (2001) 3181-3182
30. Miller J.E., Gradinaru C., Crane B.R., Di Bilio A.J., Wehbi W.A., Un S., Winkler J.R., and Gray H.B. Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment. J. Am. Chem. Soc. 125 (2003) 14220-14221
31. Crane B.R., Di Bilio A.J., Winkler J.R., and Gray H.B. Electron tunneling in single crystals of Pseudomonas aeruginosa azurins. J. Am. Chem. Soc. 123 (2001) 11623-11631
32. Nar H., Messerschmidt A., Huber R., van de Kamp M., and Canters G.W. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. J. Mol. Biol. 218 (1991) 427-447
33. Tsai L.C., Sjolin L., Langer V., Pascher T., and Nar H. Structure of the azurin mutant Phe114Ala from Pseudomonas aeruginosa at 2.6 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 51 (1995) 168-176
34. Bonander N., Leckner J., Guo H., Karlsson B.G., and Sjolin L. Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond for folding and stability?. Eur. J. Biochem. 267 (2000) 4511-4519
35. Germanas J.P., Di Bilio A.J., Gray H.B., and Richards J.H. Site saturation of the histidine-46 position in Pseudomonas aeruginosa azurin: characterization of the His46Asp copper and cobalt proteins. Biochemistry 32 (1993) 7698-7702
36. Riddles P.W., Blakeley R.L., and Zerner B. Reassessment of Ellman's reagent. Methods Enzymol. 91 (1983) 49-60
37. Bard A.J., and Faulkner L.R. Electrochemical Methods: Fundamentals and Applications (2001), John Wiley & Sons, Inc., New York
38. Trevor D.J., Chidsey C.E.D., and Loiacono D.N. In situ scanning-tunneling-microscope observation of roughening, annealing, and dissolution of gold (1 1 1) in an electrochemical cell. Phys. Rev. Lett. 62 (1989) 929-932
39. Finklea H.O. Electrochemistry of organized monolayers of thiols and related molecules on electrodes. Electroanal. Chem. 19 (1996) 109-337
40. Parry E.P., and Osteryoung R.A. Evaluation of analytical pulse polarography. Anal. Chem. 37 (1965) 1634-1637
41. Armstrong F.A., Hill H.A.O., and Walton W.J. Reactions of electron transfer proteins at electrodes. Q. Rev. Biophys. 18 (1985) 261-322
42. Pace N.C., Shirley B.A., and Thomson J.A. In: Creighton T.F. (Ed). Protein Structure: A Practical Approach (1990), IRL Press, Oxford 311-330
43. Ataka K., Richter B., and Heberle J. Orientational control of the physiological reaction of cytochrome c oxidase tethered to a gold electrode. J. Phys. Chem. B 110 (2006) 9339-9347
44. Chupa J.A., McCauley J.P., Strongin R.M., Smith III A.B., Blasie J.K., Peticolas L.J., and Bean J.C. Vectorially oriented membrane protein monolayers: profile structures via X-ray interferometry/holography. Biophys. J. 67 (1994) 336-348
45. Tronin A., Edwards A.M., Wright W.W., Vanderkooi J.M., and Blasie J.K. Orientation distributions for cytochrome c on polar and nonpolar interfaces by total internal reflection fluorescence. Biophys. J. 82 (2002) 996-1003
46. Langen R., Chang I.J., Germanas J.P., Richards J.H., Winkler J.R., and Gray H.B. Electron tunneling in proteins: coupling through a beta strand. Science 268 (1995) 1733-1735
47. Wood L.L., Cheng S.-S., Edmiston P.L., and Saavedra S.S. Molecular orientation distribution in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol-capped, self-assembled monolayers. J. Am. Chem. Soc. 119 (1997) 571-576
48. Chi Q., Zhang J., Ansersen J.E.T., and Ulstrup J. Ordered assembly and controlled electron transfer of the blue copper protein azurin at gold (1 1 1) single-crystal substrates. J. Phys. Chem. B 105 (2001) 4669-4679
49. Davis J.J., Bruce D., Canters G.W., Crozier J., and Hill H.A. Genetic modulation of metalloprotein electron transfer at bare gold. Chem. Commun. (Camb.) (2003) 576-577
50. Baymann F., Barlow N.L., Aubert C., Schoepp-Cothenet B., Leroy G., and Armstrong F.A. Voltammetry of a "protein on a rope". FEBS Lett. 539 (2003) 91-94
51. van Amsterdam I.M., Ubbink M., Einsle O., Messerschmidt A., Merli A., Cavazzini D., Rossi G.L., and Canters G.W. Dramatic modulation of electron transfer in protein complexes by crosslinking. Nat. Struct. Biol. 9 (2002) 48-52
52. Love J.C., Estroff L.A., Kriebel J.K., Nuzzo R.G., and Whitesides G.M. Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 105 (2005) 1103-1169
53. Jeuken L.J., Jones A.K., Chapman S.K., Cecchini G., and Armstrong F.A. Electron-transfer mechanisms through biological redox chains in multicenter enzymes. J. Am. Chem. Soc. 124 (2002) 5702-5713
54. Bain C.D., Troughton E.B., Tao Y.-T., Evall J., Whitesides G.M., and Nuzzo R.G. Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold. J. Am. Chem. Soc. 111 (1989) 321-335