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Volumn 111, Issue 3, 2004, Pages 229-233

An electrochemical study of hemoglobin in water-glycerol solutions

Author keywords

5 ATP; Cyclic voltammetry; Glycerol; Hemoglobin; Hydrogen peroxide; Imidazole

Indexed keywords

GLYCEROL; HEMOGLOBIN; HYDROGEN PEROXIDE; WATER;

EID: 6344261660     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.06.004     Document Type: Article
Times cited : (10)

References (20)
  • 2
    • 1842425281 scopus 로고    scopus 로고
    • Bioelectrocatalytic and enzymic activity of laccase in water-ethanol solutions, Russian
    • Bogdanovskaya V.A., Kuznetsova L.N., Tarasevich M.R. Bioelectrocatalytic and enzymic activity of laccase in water-ethanol solutions, Russian. Journal of Electrochemistry. 38:2002;1074-1081
    • (2002) Journal of Electrochemistry , vol.38 , pp. 1074-1081
    • Bogdanovskaya, V.A.1    Kuznetsova, L.N.2    Tarasevich, M.R.3
  • 3
    • 0031861753 scopus 로고    scopus 로고
    • Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques
    • Liu C.W., Bo A., Cheng G.J., Lin X.Q., Dong S.J. Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques. Biochimica et Biophysica Acta. 1385:1998;53-60
    • (1998) Biochimica et Biophysica Acta , vol.1385 , pp. 53-60
    • Liu, C.W.1    Bo, A.2    Cheng, G.J.3    Lin, X.Q.4    Dong, S.J.5
  • 4
    • 6344283552 scopus 로고    scopus 로고
    • Spectroelectrochemical study of myoglobin in DMSO
    • Mabrouk P.A., Li O.C. Spectroelectrochemical study of myoglobin in DMSO. Biochemistry-US. 40:2001;103
    • (2001) Biochemistry-US , vol.40 , pp. 103
    • Mabrouk, P.A.1    Li, O.C.2
  • 5
    • 0036746178 scopus 로고    scopus 로고
    • Enhanced electron-transfer reactivity of cytochrome b5 by dimethyl sulfoxide and N, N-dimethylformamide
    • Fan C.H., Lu J., Zhang W.J., Suzuki I., Li G.X. Enhanced electron-transfer reactivity of cytochrome b5 by dimethyl sulfoxide and N, N-dimethylformamide. Anal. Sci. 18:2002;1031-1033
    • (2002) Anal. Sci. , vol.18 , pp. 1031-1033
    • Fan, C.H.1    Lu, J.2    Zhang, W.J.3    Suzuki, I.4    Li, G.X.5
  • 6
    • 0037193185 scopus 로고    scopus 로고
    • Effect of dimethyl sulfoxide on the structure and the functional properties of horseradish peroxidase as observed by spectroscopy and cyclic voltammetry
    • Santucci R., Laurenti E., Sinibaldi F., Ferrari R.P. Effect of dimethyl sulfoxide on the structure and the functional properties of horseradish peroxidase as observed by spectroscopy and cyclic voltammetry. Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology. 1596:2002;225-233
    • (2002) Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology , vol.1596 , pp. 225-233
    • Santucci, R.1    Laurenti, E.2    Sinibaldi, F.3    Ferrari, R.P.4
  • 7
    • 0014962109 scopus 로고
    • On the structural stability and solvent denaturation of proteins: I. Denaturation by the alclhols and glycols
    • Herskovits T.T., Gadegbeku B., Jaillet H. On the structural stability and solvent denaturation of proteins: I. Denaturation by the alclhols and glycols. J. Biol. Chem. 245:1970;2588-2598
    • (1970) J. Biol. Chem. , vol.245 , pp. 2588-2598
    • Herskovits, T.T.1    Gadegbeku, B.2    Jaillet, H.3
  • 8
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko K., Timasheff S.N. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry. 20:1981;4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 9
    • 0037452644 scopus 로고    scopus 로고
    • Comparison of the redox properties of cytochrome c in aqueous and glycerol media
    • Grealis C., Magner E. Comparison of the redox properties of cytochrome c in aqueous and glycerol media. Langmuir. 19:2003;1282-1286
    • (2003) Langmuir , vol.19 , pp. 1282-1286
    • Grealis, C.1    Magner, E.2
  • 10
    • 0030573523 scopus 로고    scopus 로고
    • Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study
    • Barter M., Gaudiano M.C., Santucci R. Influence of glycerol on the structure and stability of ferric horse heart myoglobin: a SAXS and circular dichroism study. Biochimica et Biophysica Acta. 1295:1996;51-58
    • (1996) Biochimica et Biophysica Acta , vol.1295 , pp. 51-58
    • Barter, M.1    Gaudiano, M.C.2    Santucci, R.3
  • 11
    • 0033613928 scopus 로고    scopus 로고
    • Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide
    • Matsui T., Ozaki S., Liong E., Phillips G.N., Watanabe Y. Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. J. Biol. Chem. 274:1999;2838-2844
    • (1999) J. Biol. Chem. , vol.274 , pp. 2838-2844
    • Matsui, T.1    Ozaki, S.2    Liong, E.3    Phillips, G.N.4    Watanabe, Y.5
  • 12
    • 0034897798 scopus 로고    scopus 로고
    • Effect of dimethyl sulfoxide on the electron transfer reactivity of hemoglobin
    • Fan C.H., Wagner G., Li G.X. Effect of dimethyl sulfoxide on the electron transfer reactivity of hemoglobin. Bioelectrochemistry. 54:2001;49-51
    • (2001) Bioelectrochemistry , vol.54 , pp. 49-51
    • Fan, C.H.1    Wagner, G.2    Li, G.X.3
  • 14
    • 0141862126 scopus 로고    scopus 로고
    • An electrochemical investigation of effect of ATP on hemoglobin
    • Peng W.L., Liu X.J., Zhang W.J., Li G.X. An electrochemical investigation of effect of ATP on hemoglobin. Biophysical Chemistry. 106:2003;267-273
    • (2003) Biophysical Chemistry , vol.106 , pp. 267-273
    • Peng, W.L.1    Liu, X.J.2    Zhang, W.J.3    Li, G.X.4
  • 15
    • 0030042975 scopus 로고    scopus 로고
    • Electron Transfer between Electrodes and Heme Proteins in Protein-DNA Films
    • Nassar A.-E.F., Rusling J.F. Electron Transfer between Electrodes and Heme Proteins in Protein-DNA Films. J. Am. Chem. Soc. 118:1996;3043-3044
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3043-3044
    • Nassar, A.-E.F.1    Rusling, J.F.2
  • 16
    • 2442756036 scopus 로고
    • Spectrophotometric study of ionization in methaemoglobin
    • George P., Hanania G. Spectrophotometric study of ionization in methaemoglobin. Biochem. J. 55:1953;236-243
    • (1953) Biochem. J. , vol.55 , pp. 236-243
    • George, P.1    Hanania, G.2
  • 17
    • 0029645136 scopus 로고
    • Electron transfer from electrodes to myoglobin: Facilitated in sufactant films and blocked by adsorbed biomacromolecules
    • Nassar A.-E.F., Willis W.S., Rusling J.F. Electron transfer from electrodes to myoglobin: facilitated in sufactant films and blocked by adsorbed biomacromolecules. Anal. Chem. 67:1995;2386-2392
    • (1995) Anal. Chem. , vol.67 , pp. 2386-2392
    • Nassar, A.-E.F.1    Willis, W.S.2    Rusling, J.F.3
  • 18
    • 0041880443 scopus 로고    scopus 로고
    • An electrochemical investigation of ligand-binding abilities of biomimetic membrane-entrapped myoglobin
    • Zhang W.J., Fan C.H., Sun Y.T., Li G.X. An electrochemical investigation of ligand-binding abilities of biomimetic membrane-entrapped myoglobin. Biochimica et Biophysica Acta-General Subject. 1623:2003;29-32
    • (2003) Biochimica et Biophysica Acta-General Subject , vol.1623 , pp. 29-32
    • Zhang, W.J.1    Fan, C.H.2    Sun, Y.T.3    Li, G.X.4
  • 19
    • 0037034901 scopus 로고    scopus 로고
    • A model recognition switch. Electrochemical control and transduction of imidazole binding by electrode-immobilized microperoxidase-11
    • Goldston H.M., Scribner A.N., Trammell S.A., Tender L.M. A model recognition switch. Electrochemical control and transduction of imidazole binding by electrode-immobilized microperoxidase-11. Chem. Commun. 5:2002;416-417
    • (2002) Chem. Commun. , vol.5 , pp. 416-417
    • Goldston, H.M.1    Scribner, A.N.2    Trammell, S.A.3    Tender, L.M.4
  • 20
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:1970;726-734
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.