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Volumn 399, Issue 1, 2010, Pages 23-29

Investigation of the chloride effect on hemoglobin by adsorptive transfer voltammetry

Author keywords

Adsorptive transfer voltammetry; Chloride effect; Hemoglobin; Self assembled monolayer

Indexed keywords

CHLORINE COMPOUNDS; DICHROISM; ELECTRODES; HEMOGLOBIN; IONS; SELF ASSEMBLED MONOLAYERS; SURFACE PLASMON RESONANCE;

EID: 77649186473     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.10.049     Document Type: Article
Times cited : (2)

References (36)
  • 1
    • 0016614041 scopus 로고
    • The effect of potassium chloride on the Bohr effect of human hemoglobin
    • Rollema H.S., de Bruin S.H., Janssen L.H., van Os G.A. The effect of potassium chloride on the Bohr effect of human hemoglobin. J. Biol. Chem. 1975, 250:1333-1339.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1333-1339
    • Rollema, H.S.1    de Bruin, S.H.2    Janssen, L.H.3    van Os, G.A.4
  • 2
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin: haem-haem interaction and the problem of allostery
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin: haem-haem interaction and the problem of allostery. Nature 1970, 228:726-734.
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1
  • 4
    • 0016821356 scopus 로고
    • Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests
    • Chiancone E., Norne J.E., Forsen S., Bonaventura J., Brunori M., Antonini E., Wyman J. Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole-relaxation studies of hemoglobin digests. Eur. J. Biochem. 1975, 55:385-390.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 385-390
    • Chiancone, E.1    Norne, J.E.2    Forsen, S.3    Bonaventura, J.4    Brunori, M.5    Antonini, E.6    Wyman, J.7
  • 6
    • 0018572809 scopus 로고
    • X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A: evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1α
    • O'Donnell S., Mandaro R., Schuster T.M., Arnone A. X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A: evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1α. J. Biol. Chem. 1979, 254:12204-12208.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12204-12208
    • O'Donnell, S.1    Mandaro, R.2    Schuster, T.M.3    Arnone, A.4
  • 8
    • 3042660569 scopus 로고    scopus 로고
    • Electrochemical investigation of the chloride effect on hemoglobin
    • Sun Y., Liu X., Fan C., Zhang W., Li G. Electrochemical investigation of the chloride effect on hemoglobin. Bioelectrochemistry 2004, 64:23-27.
    • (2004) Bioelectrochemistry , vol.64 , pp. 23-27
    • Sun, Y.1    Liu, X.2    Fan, C.3    Zhang, W.4    Li, G.5
  • 10
    • 26444547158 scopus 로고    scopus 로고
    • Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids
    • Wang S., Chen T., Zhang Z., Shen X., Lu Z., Pang D., Wong K. Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids. Langmuir 2005, 21:9260-9266.
    • (2005) Langmuir , vol.21 , pp. 9260-9266
    • Wang, S.1    Chen, T.2    Zhang, Z.3    Shen, X.4    Lu, Z.5    Pang, D.6    Wong, K.7
  • 12
    • 54849406806 scopus 로고    scopus 로고
    • Direct electrochemistry of hemoglobin entrapped in composite electrodeposited chitosan-multiwall carbon nanotubes and nanogold particles membrane and its electrocatalytic application
    • Hu J., Liu C. Direct electrochemistry of hemoglobin entrapped in composite electrodeposited chitosan-multiwall carbon nanotubes and nanogold particles membrane and its electrocatalytic application. Electroanalysis 2008, 20:1067-1072.
    • (2008) Electroanalysis , vol.20 , pp. 1067-1072
    • Hu, J.1    Liu, C.2
  • 13
    • 48049118179 scopus 로고    scopus 로고
    • Electrochemical behaviour of haemoglobin at the liquid/liquid interface
    • Herzog G., Kam V., Arrigan D.W.M. Electrochemical behaviour of haemoglobin at the liquid/liquid interface. Electrochim. Acta 2008, 53:7204-7209.
    • (2008) Electrochim. Acta , vol.53 , pp. 7204-7209
    • Herzog, G.1    Kam, V.2    Arrigan, D.W.M.3
  • 14
    • 42649129343 scopus 로고    scopus 로고
    • Direct electrochemistry and enzymatic activity of hemoglobin immobilized in ordered mesoporous titanium oxide matrix
    • Jia N., Wen Y., Yang G., Lian Q., Xu C., Shen H. Direct electrochemistry and enzymatic activity of hemoglobin immobilized in ordered mesoporous titanium oxide matrix. Electrochem. Commun. 2008, 10:774-777.
    • (2008) Electrochem. Commun. , vol.10 , pp. 774-777
    • Jia, N.1    Wen, Y.2    Yang, G.3    Lian, Q.4    Xu, C.5    Shen, H.6
  • 16
    • 39549094231 scopus 로고    scopus 로고
    • Direct electrochemistry of hemoglobin and its electrocatalytic effect based on its direct immobilization on carbon ionic liquid electrode
    • Safavi A., Maleki N., Moradlou O., Sorouri M. Direct electrochemistry of hemoglobin and its electrocatalytic effect based on its direct immobilization on carbon ionic liquid electrode. Electrochem. Commun. 2008, 10:420-423.
    • (2008) Electrochem. Commun. , vol.10 , pp. 420-423
    • Safavi, A.1    Maleki, N.2    Moradlou, O.3    Sorouri, M.4
  • 17
    • 43649101846 scopus 로고    scopus 로고
    • Study on the combination of self-assembled electrochemical active films of hemoglobin and multilayered fibers
    • Song M., Ge L., Wang X. Study on the combination of self-assembled electrochemical active films of hemoglobin and multilayered fibers. J. Electroanal. Chem. 2008, 617:149-156.
    • (2008) J. Electroanal. Chem. , vol.617 , pp. 149-156
    • Song, M.1    Ge, L.2    Wang, X.3
  • 18
    • 15044363457 scopus 로고    scopus 로고
    • Direct electron transfer of haemoglobin and myoglobin in methanol and ethanol at didodecyldimethylammonium bromide modified pyrolytic graphite electrodes
    • Ivanova E.V., Magner E. Direct electron transfer of haemoglobin and myoglobin in methanol and ethanol at didodecyldimethylammonium bromide modified pyrolytic graphite electrodes. Electrochem. Commun. 2005, 7:323-327.
    • (2005) Electrochem. Commun. , vol.7 , pp. 323-327
    • Ivanova, E.V.1    Magner, E.2
  • 19
    • 0031061883 scopus 로고    scopus 로고
    • Films of hemoglobin and didodecyldimethylammonium bromide with enhanced electron transfer rates
    • Lu Z., Huang Q., Rusling J.F. Films of hemoglobin and didodecyldimethylammonium bromide with enhanced electron transfer rates. J. Electroanal. Chem. 1997, 423:59-66.
    • (1997) J. Electroanal. Chem. , vol.423 , pp. 59-66
    • Lu, Z.1    Huang, Q.2    Rusling, J.F.3
  • 20
    • 0035793197 scopus 로고    scopus 로고
    • Electroreduction of nitrite by hemin, myoglobin, and hemoglobin in surfactant films
    • Mimica D., Zagal J.H., Bedioui F. Electroreduction of nitrite by hemin, myoglobin, and hemoglobin in surfactant films. J. Electroanal. Chem. 2001, 497:106-113.
    • (2001) J. Electroanal. Chem. , vol.497 , pp. 106-113
    • Mimica, D.1    Zagal, J.H.2    Bedioui, F.3
  • 21
    • 22044452968 scopus 로고    scopus 로고
    • Attachment of gold nanoparticles to glassy carbon electrode and its application for the direct electrochemistry and electrocatalytic behavior of hemoglobin
    • Zhang L., Jiang X., Wang E., Dong S. Attachment of gold nanoparticles to glassy carbon electrode and its application for the direct electrochemistry and electrocatalytic behavior of hemoglobin. Biosens. Bioelectron. 2005, 21:337-345.
    • (2005) Biosens. Bioelectron. , vol.21 , pp. 337-345
    • Zhang, L.1    Jiang, X.2    Wang, E.3    Dong, S.4
  • 22
    • 20344380691 scopus 로고    scopus 로고
    • 3 nanoparticles
    • 3 nanoparticles. J. Phys. Chem. B 2005, 109:10464-10473.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 10464-10473
    • Liu, H.1    Hu, N.2
  • 23
    • 33645504413 scopus 로고    scopus 로고
    • Composite system based on chitosan and room-temperature ionic liquid: direct electrochemistry and electrocatalysis of hemoglobin
    • Lu X., Hu J., Yao X., Wang Z., Li J. Composite system based on chitosan and room-temperature ionic liquid: direct electrochemistry and electrocatalysis of hemoglobin. Biomacromolecules 2006, 7:975-980.
    • (2006) Biomacromolecules , vol.7 , pp. 975-980
    • Lu, X.1    Hu, J.2    Yao, X.3    Wang, Z.4    Li, J.5
  • 25
    • 23744448903 scopus 로고    scopus 로고
    • Core-shell nanocluster films of hemoglobin and clay nanoparticle: direct electrochemistry and electrocatalysis
    • Liu Y., Liu H., Hu N. Core-shell nanocluster films of hemoglobin and clay nanoparticle: direct electrochemistry and electrocatalysis. Biophys. Chem. 2005, 117:27-37.
    • (2005) Biophys. Chem. , vol.117 , pp. 27-37
    • Liu, Y.1    Liu, H.2    Hu, N.3
  • 26
    • 34548658001 scopus 로고    scopus 로고
    • Direct electron transfer and bioelectrocatalysis of hemoglobin on nano-structural attapulgite clay-modified glassy carbon electrode
    • Xu J., Li W., Yin Q., Zhong H., Zhu Y., Jin L. Direct electron transfer and bioelectrocatalysis of hemoglobin on nano-structural attapulgite clay-modified glassy carbon electrode. J. Colloid Interface Sci. 2007, 315:170-176.
    • (2007) J. Colloid Interface Sci. , vol.315 , pp. 170-176
    • Xu, J.1    Li, W.2    Yin, Q.3    Zhong, H.4    Zhu, Y.5    Jin, L.6
  • 28
    • 39749106132 scopus 로고    scopus 로고
    • Native, denatured, and reduced BSA: enhancement of chronopotentiometric peak H by guanidinium chloride
    • Ostatna V., Palecek E. Native, denatured, and reduced BSA: enhancement of chronopotentiometric peak H by guanidinium chloride. Electrochim. Acta 2008, 53:4014-4021.
    • (2008) Electrochim. Acta , vol.53 , pp. 4014-4021
    • Ostatna, V.1    Palecek, E.2
  • 29
    • 62349122697 scopus 로고    scopus 로고
    • Ionic strength-dependent structural transition of proteins at electrode surfaces
    • Palecek E., Ostatna V. Ionic strength-dependent structural transition of proteins at electrode surfaces. Chem. Commun. 2009, 7:1685-1687.
    • (2009) Chem. Commun. , vol.7 , pp. 1685-1687
    • Palecek, E.1    Ostatna, V.2
  • 30
    • 56749131181 scopus 로고    scopus 로고
    • Hemoglobin on phosphonic acid terminated self-assembled monolayers at a gold electrode: immobilization, direct electrochemistry, and electrocatalysis
    • Chen Y., Jin B., Guo L.R., Yang X.J., Chen W., Gu G., Zheng L.M., Xia X.H. Hemoglobin on phosphonic acid terminated self-assembled monolayers at a gold electrode: immobilization, direct electrochemistry, and electrocatalysis. Chem. Eur. J. 2008, 14:10727-10734.
    • (2008) Chem. Eur. J. , vol.14 , pp. 10727-10734
    • Chen, Y.1    Jin, B.2    Guo, L.R.3    Yang, X.J.4    Chen, W.5    Gu, G.6    Zheng, L.M.7    Xia, X.H.8
  • 32
    • 0027453843 scopus 로고
    • 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
    • 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. 1993, 233:536-545.
    • (1993) J. Mol. Biol. , vol.233 , pp. 536-545
    • Perutz, M.F.1    Fermi, G.2    Poyart, C.3    Pagnier, J.4    Kister, J.5
  • 33
    • 38549169460 scopus 로고    scopus 로고
    • Development of a heme protein structure electrochemical function database
    • Reedy C.J., Elvekrog M.M., Gibney B.R. Development of a heme protein structure electrochemical function database. Nucleic Acids Res. 2008, 36:307-313.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 307-313
    • Reedy, C.J.1    Elvekrog, M.M.2    Gibney, B.R.3
  • 34
    • 0037134780 scopus 로고    scopus 로고
    • Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry
    • Zhu Y., Cheng G., Dong S. Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry. Biophys. Chem. 2002, 97:129-138.
    • (2002) Biophys. Chem. , vol.97 , pp. 129-138
    • Zhu, Y.1    Cheng, G.2    Dong, S.3
  • 35
    • 0015239002 scopus 로고
    • Circular dichroism of hemoglobin in relation to the structure surrounding the heme
    • Sugita Y., Nagai M., Yoneyama Y. Circular dichroism of hemoglobin in relation to the structure surrounding the heme. J. Biol. Chem. 1971, 246:383-388.
    • (1971) J. Biol. Chem. , vol.246 , pp. 383-388
    • Sugita, Y.1    Nagai, M.2    Yoneyama, Y.3
  • 36
    • 39649113550 scopus 로고    scopus 로고
    • Denaturation of cytochrome c and its peroxidase activity when immobilized on SAM films
    • Wang L., Waldeck D.H. Denaturation of cytochrome c and its peroxidase activity when immobilized on SAM films. J. Phys. Chem. C 2008, 112:1351-1356.
    • (2008) J. Phys. Chem. C , vol.112 , pp. 1351-1356
    • Wang, L.1    Waldeck, D.H.2


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