메뉴 건너뛰기




Volumn 76, Issue 1-2, 2009, Pages 70-75

Electrochemistry of riboflavin-binding protein and its interaction with riboflavin

Author keywords

Constant current chronopotentiometry; Electrocatalytic peak H; Mercury and carbon electrodes; Riboflavin binding protein electrochemistry; Riboflavin protein interaction

Indexed keywords

CONSTANT CURRENT CHRONOPOTENTIOMETRY; ELECTROCATALYTIC PEAK H; MERCURY AND CARBON ELECTRODES; RIBOFLAVIN-BINDING PROTEIN ELECTROCHEMISTRY; RIBOFLAVIN-PROTEIN INTERACTION;

EID: 68549087016     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2009.04.006     Document Type: Article
Times cited : (26)

References (53)
  • 1
    • 70449291488 scopus 로고
    • The flavoprotein-apoprotein system of egg white
    • Rhodes M.B., Bennett N., and Feeney R.E. The flavoprotein-apoprotein system of egg white. J. Biol. Chem. 234 (1959) 2054-2060
    • (1959) J. Biol. Chem. , vol.234 , pp. 2054-2060
    • Rhodes, M.B.1    Bennett, N.2    Feeney, R.E.3
  • 3
    • 0019945823 scopus 로고
    • Pregnancy suppression by active immunization against gestation-specific riboflavin carrier protein
    • Murty C.V.R., and Adiga P.R. Pregnancy suppression by active immunization against gestation-specific riboflavin carrier protein. Science 216 (1982) 191-193
    • (1982) Science , vol.216 , pp. 191-193
    • Murty, C.V.R.1    Adiga, P.R.2
  • 4
    • 0021691668 scopus 로고
    • Mechanism of fetal wastage following immunoneutralization of riboflavin carrier protein in the pregnant rat - disturbances in flavin coenzyme levels
    • Krishnamurthy K., Surolia N., and Adiga P.R. Mechanism of fetal wastage following immunoneutralization of riboflavin carrier protein in the pregnant rat - disturbances in flavin coenzyme levels. FEBS Lett. 178 (1984) 87-91
    • (1984) FEBS Lett. , vol.178 , pp. 87-91
    • Krishnamurthy, K.1    Surolia, N.2    Adiga, P.R.3
  • 5
    • 0023225568 scopus 로고
    • Termination of pregnancy in mice with antiserum to chicken riboflavin-carrier protein
    • Natraj U., Kumar A., and Kadam P. Termination of pregnancy in mice with antiserum to chicken riboflavin-carrier protein. Biol. Reprod. 36 (1987) 677-685
    • (1987) Biol. Reprod. , vol.36 , pp. 677-685
    • Natraj, U.1    Kumar, A.2    Kadam, P.3
  • 6
    • 0020490684 scopus 로고
    • The binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study
    • Becvar J., and Palmer G. The binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study. J. Biol. Chem. 257 (1982) 5607-5617
    • (1982) J. Biol. Chem. , vol.257 , pp. 5607-5617
    • Becvar, J.1    Palmer, G.2
  • 7
    • 0023242454 scopus 로고
    • Positions of disulfide bonds in riboflavin protein of hen egg white
    • Hamazume Y., Mega T., and Ikenaka T. Positions of disulfide bonds in riboflavin protein of hen egg white. J. Biochem. 101 (1987) 217-223
    • (1987) J. Biochem. , vol.101 , pp. 217-223
    • Hamazume, Y.1    Mega, T.2    Ikenaka, T.3
  • 8
    • 0020009036 scopus 로고
    • Disulfide bonds in egg-white riboflavin-binding protein. Chemical reduction studies
    • Kozik A. Disulfide bonds in egg-white riboflavin-binding protein. Chemical reduction studies. Eur. J. Biochem. 121 (1982) 395-400
    • (1982) Eur. J. Biochem. , vol.121 , pp. 395-400
    • Kozik, A.1
  • 9
    • 0017699806 scopus 로고
    • A fluorescence study of egg white riboflavin-binding protein
    • Nishina Y., Horiike K., Shiga K., and Yamano T. A fluorescence study of egg white riboflavin-binding protein. J. Biochem. 82 (1977) 1715-1721
    • (1977) J. Biochem. , vol.82 , pp. 1715-1721
    • Nishina, Y.1    Horiike, K.2    Shiga, K.3    Yamano, T.4
  • 10
    • 84989695139 scopus 로고
    • Fluorescence quenching for flavins interacting with egg white riboflavin-binding protein
    • Bystra-Mieloszyk K., Balter A., and Drabent R. Fluorescence quenching for flavins interacting with egg white riboflavin-binding protein. Photochem. Photobiol. 41 (1985) 141-147
    • (1985) Photochem. Photobiol. , vol.41 , pp. 141-147
    • Bystra-Mieloszyk, K.1    Balter, A.2    Drabent, R.3
  • 11
    • 0000253289 scopus 로고
    • Methods used to reversibly resolve flavoproteins into the constituents apoflavoprotein and prosthetic group
    • Müller F. (Ed), CRC Press, Boca Raton, FL
    • Müller F., and van Berkel W.J.H. Methods used to reversibly resolve flavoproteins into the constituents apoflavoprotein and prosthetic group. In: Müller F. (Ed). Chemistry and Biochemistry of Flavoenzymes (1991), CRC Press, Boca Raton, FL 261-274
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 261-274
    • Müller, F.1    van Berkel, W.J.H.2
  • 12
    • 0015447257 scopus 로고
    • Riboflavin carrier protein from egg yolk. Spectral and other properties observed upon binding of flavin to apoprotein
    • Zak Z., Ostrowski W., Steczko J., Weber M., Gizler M., and Morawiecki A. Riboflavin carrier protein from egg yolk. Spectral and other properties observed upon binding of flavin to apoprotein. Acta Biochim. Pol. 19 (1972) 307-323
    • (1972) Acta Biochim. Pol. , vol.19 , pp. 307-323
    • Zak, Z.1    Ostrowski, W.2    Steczko, J.3    Weber, M.4    Gizler, M.5    Morawiecki, A.6
  • 13
    • 0017912989 scopus 로고
    • Riboflavin binding in egg-white flavoprotein: role of tryptophan and tyrosine
    • Blankenhorn G. Riboflavin binding in egg-white flavoprotein: role of tryptophan and tyrosine. Eur. J. Biochem. 82 (1978) 155-160
    • (1978) Eur. J. Biochem. , vol.82 , pp. 155-160
    • Blankenhorn, G.1
  • 16
    • 68549093461 scopus 로고
    • The riboflavin flavoprotein from egg yolk
    • Ostrowski W., and Krawczyk A. The riboflavin flavoprotein from egg yolk. Acta Chem. Scand. 17 (1963) 241-245
    • (1963) Acta Chem. Scand. , vol.17 , pp. 241-245
    • Ostrowski, W.1    Krawczyk, A.2
  • 18
    • 0000353359 scopus 로고
    • Polarographic studies with the dropping mercury cathode. Part XIII. The effect of albumins
    • Heyrovsky J., and Babicka J. Polarographic studies with the dropping mercury cathode. Part XIII. The effect of albumins. Collect. Czechoslov. Chem. Commun. 2 (1930) 370-379
    • (1930) Collect. Czechoslov. Chem. Commun. , vol.2 , pp. 370-379
    • Heyrovsky, J.1    Babicka, J.2
  • 21
    • 0001632936 scopus 로고    scopus 로고
    • Constant current chronopotentiometric stripping analysis of bioactive peptides at mercury and carbon electrodes
    • Tomschik M., Havran L., Fojta M., and Palecek E. Constant current chronopotentiometric stripping analysis of bioactive peptides at mercury and carbon electrodes. Electroanalysis 10 (1998) 403-409
    • (1998) Electroanalysis , vol.10 , pp. 403-409
    • Tomschik, M.1    Havran, L.2    Fojta, M.3    Palecek, E.4
  • 23
    • 36849009766 scopus 로고    scopus 로고
    • Chronopotentiometric determination of redox states of peptides
    • Dorcak V., and Palecek E. Chronopotentiometric determination of redox states of peptides. Electroanalysis 19 (2007) 2405-2412
    • (2007) Electroanalysis , vol.19 , pp. 2405-2412
    • Dorcak, V.1    Palecek, E.2
  • 24
    • 54549087895 scopus 로고    scopus 로고
    • Constant current chronopotentiometry and voltammetry of native and denatured serum albumin at mercury and carbon electrodes
    • Ostatna V., Kuralay F., Trnkova L., and Palecek E. Constant current chronopotentiometry and voltammetry of native and denatured serum albumin at mercury and carbon electrodes. Electroanalysis 20 (2008) 1406-1413
    • (2008) Electroanalysis , vol.20 , pp. 1406-1413
    • Ostatna, V.1    Kuralay, F.2    Trnkova, L.3    Palecek, E.4
  • 25
    • 39749106132 scopus 로고    scopus 로고
    • Native, denatured and reduced BSA - enhancement of chronopotentiometric peak H by guanidinium chloride
    • Ostatna V., and Palecek E. Native, denatured and reduced BSA - enhancement of chronopotentiometric peak H by guanidinium chloride. Electrochim. Acta 53 (2008) 4014-4021
    • (2008) Electrochim. Acta , vol.53 , pp. 4014-4021
    • Ostatna, V.1    Palecek, E.2
  • 26
    • 33745812035 scopus 로고    scopus 로고
    • Native and denatured bovine serum albumin. D.c. polarography, stripping voltammetry and constant current chronopotentiometry
    • Ostatna V., Uslu B., Dogan B., Ozkan S., and Palecek E. Native and denatured bovine serum albumin. D.c. polarography, stripping voltammetry and constant current chronopotentiometry. J. Electroanal. Chem. 593 (2006) 172-178
    • (2006) J. Electroanal. Chem. , vol.593 , pp. 172-178
    • Ostatna, V.1    Uslu, B.2    Dogan, B.3    Ozkan, S.4    Palecek, E.5
  • 27
    • 36849060322 scopus 로고    scopus 로고
    • Electroactivity of nonconjugated proteins and peptides. Towards electroanalysis of all proteins
    • Palecek E., and Ostatna V. Electroactivity of nonconjugated proteins and peptides. Towards electroanalysis of all proteins. Electroanalysis 19 (2007) 2383-2403
    • (2007) Electroanalysis , vol.19 , pp. 2383-2403
    • Palecek, E.1    Ostatna, V.2
  • 28
    • 37249075450 scopus 로고    scopus 로고
    • Changes in interfacial properties of α-synuclein preceding its aggregation
    • Palecek E., Ostatna V., Masarik M., Bertoncini C.W., and Jovin T.M. Changes in interfacial properties of α-synuclein preceding its aggregation. Analyst 133 (2008) 76-84
    • (2008) Analyst , vol.133 , pp. 76-84
    • Palecek, E.1    Ostatna, V.2    Masarik, M.3    Bertoncini, C.W.4    Jovin, T.M.5
  • 29
    • 60549098838 scopus 로고    scopus 로고
    • Interaction of biomacromolecules with surfaces viewed by electrochemical methods
    • Dorcak V., Bartosik M., Ostatna V., Palecek E., and Heyrovsky M. Interaction of biomacromolecules with surfaces viewed by electrochemical methods. Electroanalysis 21 (2009) 662-665
    • (2009) Electroanalysis , vol.21 , pp. 662-665
    • Dorcak, V.1    Bartosik, M.2    Ostatna, V.3    Palecek, E.4    Heyrovsky, M.5
  • 30
    • 62349122697 scopus 로고    scopus 로고
    • Ionic strength-dependent structural transition of proteins at electrode surfaces
    • Palecek E., and Ostatna V. Ionic strength-dependent structural transition of proteins at electrode surfaces. Chem. Commun. (2009) 1685-1687
    • (2009) Chem. Commun. , pp. 1685-1687
    • Palecek, E.1    Ostatna, V.2
  • 32
    • 68549114376 scopus 로고
    • The polarographic catalytic wave of riboflavin
    • Jambor B. The polarographic catalytic wave of riboflavin. Acta Chim. Hung. 48 (1966) 89-98
    • (1966) Acta Chim. Hung. , vol.48 , pp. 89-98
    • Jambor, B.1
  • 34
    • 68549124259 scopus 로고
    • Katalytische Wasserstoffausscheidung an einer Quecksilbertropfelektrode durch Einwirkung von Riboflavin und seinen Derivaten
    • Knobloch E. Katalytische Wasserstoffausscheidung an einer Quecksilbertropfelektrode durch Einwirkung von Riboflavin und seinen Derivaten. Collect. Czechoslov. Chem. Commun. 31 (1966) 4503-4516
    • (1966) Collect. Czechoslov. Chem. Commun. , vol.31 , pp. 4503-4516
    • Knobloch, E.1
  • 35
    • 0004223208 scopus 로고
    • Isoalloxazines, flavins and flavin nucleotides
    • Dryhurst G. (Ed), Academic Press, New York
    • Dryhurst G. Isoalloxazines, flavins and flavin nucleotides. In: Dryhurst G. (Ed). Electrochemistry of Biological Molecules (1977), Academic Press, New York 365-391
    • (1977) Electrochemistry of Biological Molecules , pp. 365-391
    • Dryhurst, G.1
  • 36
    • 4544352686 scopus 로고    scopus 로고
    • Electroactivity of avidin and streptavidin. Avidin signals at mercury and carbon electrodes respond to biotin binding
    • Havran L., Billova S., and Palecek E. Electroactivity of avidin and streptavidin. Avidin signals at mercury and carbon electrodes respond to biotin binding. Electroanalysis 16 (2004) 1139-1148
    • (2004) Electroanalysis , vol.16 , pp. 1139-1148
    • Havran, L.1    Billova, S.2    Palecek, E.3
  • 37
    • 62349121113 scopus 로고    scopus 로고
    • Electrochemical determination of thioredoxin redox states
    • Dorcak V., and Palecek E. Electrochemical determination of thioredoxin redox states. Anal. Chem. 81 (2009) 1543-1548
    • (2009) Anal. Chem. , vol.81 , pp. 1543-1548
    • Dorcak, V.1    Palecek, E.2
  • 38
    • 0034521659 scopus 로고    scopus 로고
    • Binding study of riboflavin-binding protein with riboflavin and its analogues by differential scanning calorimetry
    • Wasylewski M. Binding study of riboflavin-binding protein with riboflavin and its analogues by differential scanning calorimetry. J. Protein Chem. 19 (2000) 523-528
    • (2000) J. Protein Chem. , vol.19 , pp. 523-528
    • Wasylewski, M.1
  • 39
    • 49149145521 scopus 로고
    • Electrochemical oxidation of nucleic acids and proteins at graphite electrode. Qualitative aspects
    • Brabec V. Electrochemical oxidation of nucleic acids and proteins at graphite electrode. Qualitative aspects. Bioelectrochem. Bioenerg. 7 (1980) 69-82
    • (1980) Bioelectrochem. Bioenerg. , vol.7 , pp. 69-82
    • Brabec, V.1
  • 40
    • 0000577514 scopus 로고
    • The electrochemical oxidation of three proteins: RNAase A, bovine serum albumin and concanavalin A at solid electrodes
    • Reynaud J.A., Malfoy B., and Bere A. The electrochemical oxidation of three proteins: RNAase A, bovine serum albumin and concanavalin A at solid electrodes. Bioelectrochem. Bioenerg. 7 (1980) 595-606
    • (1980) Bioelectrochem. Bioenerg. , vol.7 , pp. 595-606
    • Reynaud, J.A.1    Malfoy, B.2    Bere, A.3
  • 41
    • 0030579065 scopus 로고    scopus 로고
    • Potentiometric stripping analysis of bioactive peptides at carbon electrodes down to subnanomolar concentrations
    • Cai X.H., Rivas G., Farias P.A.M., Shiraishi H., Wang J., and Palecek E. Potentiometric stripping analysis of bioactive peptides at carbon electrodes down to subnanomolar concentrations. Anal. Chim. Acta 332 (1996) 49-57
    • (1996) Anal. Chim. Acta , vol.332 , pp. 49-57
    • Cai, X.H.1    Rivas, G.2    Farias, P.A.M.3    Shiraishi, H.4    Wang, J.5    Palecek, E.6
  • 42
    • 77956691190 scopus 로고    scopus 로고
    • Catalytic hydrogen evolution on mercury electrodes from solutions of peptides and proteins
    • Palecek E., Scheller F., and Wang J. (Eds), Elsevier, Amsterdam
    • Heyrovsky M. Catalytic hydrogen evolution on mercury electrodes from solutions of peptides and proteins. In: Palecek E., Scheller F., and Wang J. (Eds). Electrochemistry of Nucleic Acids and Proteins. Towards Electrochemical Sensors for Genomics and Proteomics (2005), Elsevier, Amsterdam 657-687
    • (2005) Electrochemistry of Nucleic Acids and Proteins. Towards Electrochemical Sensors for Genomics and Proteomics , pp. 657-687
    • Heyrovsky, M.1
  • 44
    • 60549095880 scopus 로고    scopus 로고
    • 50 years of nucleic acid electrochemistry
    • Palecek E. 50 years of nucleic acid electrochemistry. Electroanalysis 21 (2009) 239-251
    • (2009) Electroanalysis , vol.21 , pp. 239-251
    • Palecek, E.1
  • 45
    • 0000480753 scopus 로고
    • Normal pulse polarography of double-helical DNA: dependence of the wave height on starting potential
    • Palecek E. Normal pulse polarography of double-helical DNA: dependence of the wave height on starting potential. Collect. Czechoslov. Chem. Commun. 39 (1974) 3449-3455
    • (1974) Collect. Czechoslov. Chem. Commun. , vol.39 , pp. 3449-3455
    • Palecek, E.1
  • 46
    • 0002790964 scopus 로고
    • Adsorptive transfer stripping voltammetry. Effect of the electrode potential on the structure of DNA adsorbed at the mercury surface
    • Palecek E. Adsorptive transfer stripping voltammetry. Effect of the electrode potential on the structure of DNA adsorbed at the mercury surface. Bioelectrochem. Bioenerg. 28 (1992) 71-83
    • (1992) Bioelectrochem. Bioenerg. , vol.28 , pp. 71-83
    • Palecek, E.1
  • 47
    • 0000603482 scopus 로고    scopus 로고
    • Direct electrochemistry of cytochrome c
    • Scott R.A., and Mauk A.G. (Eds), University Science Books, Sausalito
    • Hill H.A.O., Guo L.H., and McLendon G. Direct electrochemistry of cytochrome c. In: Scott R.A., and Mauk A.G. (Eds). Cytochrome C: A Multidisciplinary Approach (1996), University Science Books, Sausalito 317-333
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 317-333
    • Hill, H.A.O.1    Guo, L.H.2    McLendon, G.3
  • 48
    • 4544231695 scopus 로고    scopus 로고
    • Direct peroxidase bioelectrocatalysis on a variety of electrode materials
    • Ferapontova E.E. Direct peroxidase bioelectrocatalysis on a variety of electrode materials. Electroanalysis 16 (2004) 1101-1112
    • (2004) Electroanalysis , vol.16 , pp. 1101-1112
    • Ferapontova, E.E.1
  • 52
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • Leger C., and Bertrand P. Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chem. Rev. 108 (2008) 2379-2438
    • (2008) Chem. Rev. , vol.108 , pp. 2379-2438
    • Leger, C.1    Bertrand, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.