Electrochemical investigation of the chloride effect on hemoglobin

Bioelectrochemistry

Volumn 64, Issue 1, 2004, Pages 23-27

  Sun, Yuting ^a   Liu, Xinjian ^a   Fan, Chunhai ^a   Zhang, Wenjun ^a   Li, Genxi ^a  

^a NANJING UNIVERSITY   (China)

Author keywords

Allosteric effect; Chloride; Direct electrochemistry; Hemoglobin

Indexed keywords

ADDITION REACTIONS; CHLORINE; ELECTRODES; GOLD; HEMOGLOBIN; PROTEINS;

ELECTROCHEMICAL RESPONSE; ELECTRON TRANSFER; TERTIARY STRUCTURES;

ELECTROCHEMISTRY;

4,4' BIPYRIDINE; CHLORIDE; HEMOGLOBIN;

ARTICLE; CHEMICAL BINDING; ELECTROCHEMICAL DETECTION; ELECTROCHEMISTRY; ELECTRODE; ELECTRON TRANSPORT; HEMOGLOBIN DETERMINATION; PROTEIN STRUCTURE;

ANIMALS; CATTLE; CHLORIDES; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROCHEMISTRY; ELECTRODES; ELECTRON TRANSPORT; GOLD; HEMOGLOBINS; POTENTIOMETRY; SPECTRUM ANALYSIS;

EID: 3042660569     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2004.01.003     Document Type: Article

References (31)

1. Perutz M.F., Wilkinson A.J., Paoli M., Dodson G.G. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu. Rev. Biophys. Biomol. Struct. 27:1998;1-34
2. Perutz M.F. Nature of haem-haem interaction. Nature. 237:1972;495-499
3. Ackers G.K., Doyle M.L., Myers D., Daugherty M.A. Molecular code for cooperativity in hemoglobin. Science. 255:1992;54-63
4. Schumacher M.A., Dixon M.M., Kluger R., Jones R.T., Brennan R.G. Allosteric transition intermediates modeled by crosslinked haemoglobins. Nature. 375:1995;84-87
5. Hultquist D.E., Sannes L.J., Juckett D.A. Catalysis of methemoglobin reduction. Curr. Top. Cell. Regul. 24:1984;287-300
6. Sun W., Kong J., Deng J. Electrocatalytic reduction of hemoglobin at a chemically modified electrode containing riboflavin. Electroanalysis. 9:1997;115-119
7. Eddowes M.J., Hill H.A.O. Novel method for the investigation of the electrochemistry of metalloproteins: cytochrome c. J. Chem. Soc., Chem. Commun. 21:1977;771-772
8. Ye J., Baldwin R.P. Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. Anal. Chem. 60:1988;2263-2268
9. Song S., Dong S. Spectroelectrochemistry of the quasi-reversible reduction and oxidation of hemoglobin at a methylene blue adsorbed modified electrode. Bioelectrochem. Bioenerg. 19:1988;337-346
10. Fan C., Wang H., Sun S., Zhu D., Wagner G., Li G. Electron transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane. Anal. Chem. 73:2001;2850-2854
11. Zhu Y., Dong S. Rapid oxidation and reduction of hemoglobin at a bifunctional dye of Janus Green modified electrode. Bioelectrochem. Bioenerg. 24:1990;23-31
12. Dong S., Zhu Y., Song S. Electrode processes of hemoglobin at a platinum electrode covered by Brilliant Cresyl Blue. Bioelectrochem. Bioenerg. 21:1989;233-243
13. Dong S., Chu Q. Study of the electrode process of hemoglobin at a polymerized Azure A film electrode. Electroanalysis. 5:1993;135-140
14. Ju H., Dong L., Chen H. Electrocatalytic behavior of Toluidine Blue O covalently modified microcylinder carbon fiber electrode and amperometric determination of hemoglobin in whole blood. Anal. Lett. 29:1996;587-599
15. Kuramitz H., Sugawara K., Kawasaki M., Hasebe K., Nakamura H., Tanaka S. Electrocatalytic reduction of hemoglobin at a self-assembled monolayer electrode containing redox dye, Nile Blue as an electron-transfer mediator. Anal. Sci. 15:1999;589-592
16. Rusling J.F. Enzyme bioelectrochemistry in cast biomembrane-like films. Acc. Chem. Res. 31:1998;363-369
17. Yang J., Hu N. Direct electron transfer for hemoglobin in biomembrane-like dimyristoyl phosphatidylcholine films on pyrolytic graphite electrodes. Bioelectrochem. Bioenerg. 48:1999;117-127
18. Chen X., Hu N., Zeng Y., Rusling J.F., Yang J. Ordered electrochemically active films of hemoglobin, didodecyldimethylammonium ions, and clay. Langmuir. 15:1999;7022-7030
19. Perutz M.F., Shih D.T.-B., Williamson D. The chloride effect in human haemoglobin, a new kind of allosteric mechanism. J. Mol. Biol. 239:1994;555-560
20. Fronticelli C., Sanna M.T., Perez-Alvarado G.C., Karavitis M., Lu A.-L., Brinigar W.S. Allosteric modulation by tertiary structure in mammalian hemoglobins. J. Biol. Chem. 270:1995;30588-30592
21. Manjula B.N., Malavalli A., Prabhakaran M., Friedman J.M., Acharya A.S. Activation of the low oxygen affinity-inducing potential of the Asn108 (β) Lys mutation of Hb-presbyterian on intramolecular αα-fumaryl cross-bridging. Protein Eng. 14:2001;359-366
22. Ferri T., Poscia A., Ascoli F., Santucci R. Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c. Biochim. Biophys. Acta. 1298:1996;102-108
23. Kataoka M., Hagihara Y., Mihara K., Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229:1993;591-596
24. Nassar A.-E.F., Zhang Z., Hu N., Rusling J.F., Kumosinski T.F. Proton-coupled electron transfer from electrodes to myoglobin in ordered biomembrane-like films. J. Phys. Chem., B. 101:1997;2224-2231
25. Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J. A novel allosteric mechanism in haemoglobin: structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked bohr effect in bovine and human haemoglobin. J. Mol. Biol. 233:1993;536-545
26. Lu T., Yu X., Dong S., Zhou C., Ye S., Cotton T.M. Direct electrochemical reactions of cytochrome c at iodide-modified electrodes. J. Electroanal. Chem. 369:1994;79-86
27. 2 binding. Biochemistry. 38:1999;11741-11748
28. Nassar A.-E.F., Willis W.S., Rusling J.F. Electron transfer from electrodes to myoglobin: facilitated in surfactant films and blocked by adsorbed biomacromolecules. Anal. Chem. 67:1995;2386-2392
29. Eddowes M.J., Hill H.A.O., Uosaki K. The electrochemistry of cytochrome c investigation of the mechanism of the 4, 4′-bipyridyl surface modified gold electrode. Bioelectrochem. Bioenerg. 7:1980;527-537
30. Murray R.W. Bard A.J. Chemically Modified Electrodes, Electroanalytical Chemistry. vol. 13:1984;191-368 Marcel Dekker, New York
31. Sun D.P., Zou M., Ho N.T., Ho C. Contribution of surface histidyl residues in the α-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effects. Biochemistry. 36:1997;6663-6673