메뉴 건너뛰기




Volumn 181, Issue 1-3, 2008, Pages 179-187

Mössbauer spectroscopic evidence on the heme binding to the proximal histidine in unfolded carbonmonoxy myoglobin by guanidine hydrochloride

Author keywords

Carbonmonoxy myoglobin; Guanidine hydrochloride; Isomer shift; M ssbauer spectroscopy; Unfolding

Indexed keywords


EID: 54849416377     PISSN: 03043843     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10751-008-9711-z     Document Type: Article
Times cited : (2)

References (33)
  • 2
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • C.B. Anfinsen H.A. Scheraga 1975 Experimental and theoretical aspects of protein folding Adv. Protein Chem. 29 205 300
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 4
    • 0028290594 scopus 로고
    • Acid-induced folding of heme proteins
    • Y. Goto A.L. Fink 1994 Acid-induced folding of heme proteins Methods Enzymol. 232 3 15
    • (1994) Methods Enzymol. , vol.232 , pp. 3-15
    • Goto, Y.1    Fink, A.L.2
  • 6
    • 0014364651 scopus 로고
    • Protein denaturation
    • C. Tanford 1968 Protein denaturation Adv. Protein Chem. 23 121 283
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-283
    • Tanford, C.1
  • 7
    • 0014939368 scopus 로고
    • The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
    • Y. Nozaki C. Tanford 1970 The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions J. Biol. Chem. 245 1648 1653
    • (1970) J. Biol. Chem. , vol.245 , pp. 1648-1653
    • Nozaki, Y.1    Tanford, C.2
  • 9
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace 1986 Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 11
    • 0018798895 scopus 로고
    • Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin
    • C.N. Pace K.E. Vanderburg 1979 Determining globular protein stability: Guanidine hydrochloride denaturation of myoglobin Biochemistry 18 288 292
    • (1979) Biochemistry , vol.18 , pp. 288-292
    • Pace, C.N.1    Vanderburg, K.E.2
  • 12
    • 0001062291 scopus 로고
    • Kinetic studies on the reaction between native globin and haem derivatives
    • Q.H. Gibson E. Antonini 1960 Kinetic studies on the reaction between native globin and haem derivatives Biochem. J. 77 328 341
    • (1960) Biochem. J. , vol.77 , pp. 328-341
    • Gibson, Q.H.1    Antonini, E.2
  • 14
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • M.S. Hargrove J.S. Olson 1996 The stability of holomyoglobin is determined by heme affinity Biochemistry 35 11310 11318
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 15
    • 0020533291 scopus 로고
    • The kinetic mechanism of heme binding to human apohemoglobin
    • M.Y. Rose J.S. Olson 1983 The kinetic mechanism of heme binding to human apohemoglobin J. Biol. Chem. 258 4298 4303
    • (1983) J. Biol. Chem. , vol.258 , pp. 4298-4303
    • Rose, M.Y.1    Olson, J.S.2
  • 16
    • 0015498969 scopus 로고
    • Kinetics of conformation change of sperm-whale myoglobin.I. folding and unfolding of metmyoglobin following pH jump
    • L.L. Shen J. Hermans Jr. 1972 Kinetics of conformation change of sperm-whale myoglobin.I. folding and unfolding of metmyoglobin following pH jump Biochemistry 11 1836 1841
    • (1972) Biochemistry , vol.11 , pp. 1836-1841
    • Shen, L.L.1    Hermans Jr., J.2
  • 17
    • 0015498936 scopus 로고
    • Kinetics of conformation change of sperm-whale myoglobin.II. characterization of the rapidly and slowly formed denatured species(D and D*)
    • L.L. Shen J. Hermans Jr. 1972 Kinetics of conformation change of sperm-whale myoglobin.II. characterization of the rapidly and slowly formed denatured species(D and D*) Biochemistry 11 1842 1844
    • (1972) Biochemistry , vol.11 , pp. 1842-1844
    • Shen, L.L.1    Hermans Jr., J.2
  • 18
    • 0022244852 scopus 로고
    • Complexities in the denaturation of horse metmyoglobin by guanidine hydrochloride
    • F. Ahmad 1985 Complexities in the denaturation of horse metmyoglobin by guanidine hydrochloride J. Biol. Chem. 260 10458 10460
    • (1985) J. Biol. Chem. , vol.260 , pp. 10458-10460
    • Ahmad, F.1
  • 19
    • 0024277369 scopus 로고
    • Reconstitution of myoglobin from apoprotein and heme, monitored by stopped-flow absorption, fluorescence and circular dichroism
    • Y. Kawamura-Konishi H. Kihara H. Suzuki 1988 Reconstitution of myoglobin from apoprotein and heme, monitored by stopped-flow absorption, fluorescence and circular dichroism Eur. J. Biochem. 170 589 595
    • (1988) Eur. J. Biochem. , vol.170 , pp. 589-595
    • Kawamura-Konishi, Y.1    Kihara, H.2    Suzuki, H.3
  • 20
    • 0026688996 scopus 로고
    • Kinetics of the reconstitution of hemoglobin from semihemoglobins and β with heme
    • Y. Kawamura-Konishi K. Chiba H. Kihara H. Suzuki 1992 Kinetics of the reconstitution of hemoglobin from semihemoglobins and β with heme Eur. Biophys. J. 21 85 92
    • (1992) Eur. Biophys. J. , vol.21 , pp. 85-92
    • Kawamura-Konishi, Y.1    Chiba, K.2    Kihara, H.3    Suzuki, H.4
  • 21
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • M.S. Hargrove D. Barrick J.S. Olson 1996 The association rate constant for heme binding to globin is independent of protein structure Biochemistry 35 11293 11299
    • (1996) Biochemistry , vol.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 22
    • 0037183066 scopus 로고    scopus 로고
    • Denaturation of a protein monitored by diffusion coefficients: Myoglobin
    • J. Choi M. Terajima 2002 Denaturation of a protein monitored by diffusion coefficients: myoglobin J. Phys. Chem. B. 106 6587 6593
    • (2002) J. Phys. Chem. B. , vol.106 , pp. 6587-6593
    • Choi, J.1    Terajima, M.2
  • 23
    • 0014413956 scopus 로고
    • Spectral studies on the denaturation of myoglobin
    • A.N. Schechter C.J. Epstein 1968 Spectral studies on the denaturation of myoglobin J. Mol. Biol. 35 567 589
    • (1968) J. Mol. Biol. , vol.35 , pp. 567-589
    • Schechter, A.N.1    Epstein, C.J.2
  • 25
    • 0034708714 scopus 로고    scopus 로고
    • Heme orientation affects holo-myoglobin folding and unfolding kinetics
    • C. Moczygemba J. Guidry P. Wittung-Stafshede 2000 Heme orientation affects holo-myoglobin folding and unfolding kinetics FEBS Lett. 470 203 206
    • (2000) FEBS Lett. , vol.470 , pp. 203-206
    • Moczygemba, C.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 26
    • 0014743042 scopus 로고
    • Mössbauer spectroscopy of haem proteins
    • G. Lang 1970 Mössbauer spectroscopy of haem proteins Quart. Rev. Biophys. 3 1 60
    • (1970) Quart. Rev. Biophys. , vol.3 , pp. 1-60
    • Lang, G.1
  • 29
    • 0019763671 scopus 로고
    • Preparation and properties of apohemoglobin and reconstituted hemoglobin
    • F. Ascoli M.R. Rossi-Fanelli E. Antonini 1981 Preparation and properties of apohemoglobin and reconstituted hemoglobin Methods Enzymol. 76 72
    • (1981) Methods Enzymol. , vol.76 , pp. 72
    • Ascoli, F.1    Rossi-Fanelli, M.R.2    Antonini, E.3
  • 31
    • 0015505877 scopus 로고
    • Mössbauer studies on oxo-bridged iron(III) porphines
    • M.A. Torréns D.K. Straub L.M. Epstein 1972 Mössbauer studies on oxo-bridged iron(III) porphines J. Am. Chem. Soc. 94 4160 4162
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 4160-4162
    • Torréns, M.A.1    Straub, D.K.2    Epstein, L.M.3
  • 32
    • 0025855421 scopus 로고
    • Spectroscopic studies of myoglobin at low pH: Heme structure and ligation
    • J.T. Sage D. Morikis P.M. Champion 1991 Spectroscopic studies of myoglobin at low pH: heme structure and ligation Biochemistry 30 1227 1237
    • (1991) Biochemistry , vol.30 , pp. 1227-1237
    • Sage, J.T.1    Morikis, D.2    Champion, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.