메뉴 건너뛰기




Volumn 235, Issue 1-2, 1996, Pages 49-53

Kinetic evidence for the existence of a rate-limiting step in the reaction of ferric hemoproteins with anionic ligands

Author keywords

azide binding; conformational transition; ferric hemoproteins; kinetics

Indexed keywords

HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN;

EID: 0030042056     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00049.x     Document Type: Article
Times cited : (32)

References (26)
  • 4
    • 0022407823 scopus 로고
    • The CO bond angle of carboxymyoglobin determined by angular-resolved XANES spectroscopy
    • Bianconi, A., Congiu Castellano, A., Durham, P. J., Hasnain, S. S. & Phillips, S. (1985) The CO bond angle of carboxymyoglobin determined by angular-resolved XANES spectroscopy, Nature 318, 685-687.
    • (1985) Nature , vol.318 , pp. 685-687
    • Bianconi, A.1    Congiu Castellano, A.2    Durham, P.J.3    Hasnain, S.S.4    Phillips, S.5
  • 8
    • 0019738499 scopus 로고
    • Preparation of isolated chains of human hemoglobin
    • Bucci, E. (1981) Preparation of isolated chains of human hemoglobin, Methods Enzymol. 76, 97-106.
    • (1981) Methods Enzymol. , vol.76 , pp. 97-106
    • Bucci, E.1
  • 10
    • 0023660124 scopus 로고
    • 1H nuclear magnetic resonance spectrum of carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques
    • 1H nuclear magnetic resonance spectrum of carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques, J. Mol. Biol. 194, 313-327.
    • (1987) J. Mol. Biol. , vol.194 , pp. 313-327
    • Dalvit, C.1    Wright, P.E.2
  • 13
    • 0025250645 scopus 로고
    • Interaction of hemoglobin with chloride and 2,3-biphosphoglycerate. A comparative approach
    • Giardina, B., Brix, O., Colosimo, A., Petruzzelli, R., Cerroni, L. & Condo', S. G. (1990) Interaction of hemoglobin with chloride and 2,3-biphosphoglycerate. A comparative approach, Eur. J. Biochem. 194, 61-65.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 61-65
    • Giardina, B.1    Brix, O.2    Colosimo, A.3    Petruzzelli, R.4    Cerroni, L.5    Condo', S.G.6
  • 14
    • 0014670534 scopus 로고
    • The reaction of methemoglobin with some ligands
    • Gibson, Q. H., Parkhurst, L. J. & Geraci, G. (1969) The reaction of methemoglobin with some ligands, J. Biol. Chem. 244, 4668-4673.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4668-4673
    • Gibson, Q.H.1    Parkhurst, L.J.2    Geraci, G.3
  • 16
    • 77957095245 scopus 로고
    • Nonlinear least-squares analysis
    • Johnson, M. L. & Frasier, S. G. (1985) Nonlinear least-squares analysis, Methods Enzymol. 117, 301-342.
    • (1985) Methods Enzymol. , vol.117 , pp. 301-342
    • Johnson, M.L.1    Frasier, S.G.2
  • 17
    • 0024974675 scopus 로고
    • Structure of myoglobin-ethyl isocyanide. Histidine as a swinging door for ligand entry
    • Johnson, K., Olson, J. S. & Phillips, G. N. Jr (1989) Structure of myoglobin-ethyl isocyanide. Histidine as a swinging door for ligand entry, J. Mol. Biol. 207, 459-463.
    • (1989) J. Mol. Biol. , vol.207 , pp. 459-463
    • Johnson, K.1    Olson, J.S.2    Phillips Jr., G.N.3
  • 18
    • 0017736964 scopus 로고
    • The structure of horse methaemoglobin at 2.0 Å resolution
    • Ladner, R. C., Heidner, E. J. & Perutz, M. F. (1977) The structure of horse methaemoglobin at 2.0 Å resolution, J. Mol. Biol. 114, 385-414.
    • (1977) J. Mol. Biol. , vol.114 , pp. 385-414
    • Ladner, R.C.1    Heidner, E.J.2    Perutz, M.F.3
  • 19
    • 0026022973 scopus 로고
    • X-ray crystal structure of the ferric sperm whale myoglobin:imidazole complex at 2.0 Å resolution
    • Lionetti, C., Guanziroli, M. G., Frigerio, F., Ascenzi, P. & Bolognesi, M. (1991) X-ray crystal structure of the ferric sperm whale myoglobin:imidazole complex at 2.0 Å resolution, J. Mol. Biol. 217, 409-412.
    • (1991) J. Mol. Biol. , vol.217 , pp. 409-412
    • Lionetti, C.1    Guanziroli, M.G.2    Frigerio, F.3    Ascenzi, P.4    Bolognesi, M.5
  • 20
    • 0017812334 scopus 로고
    • Unusually fast ligand exchange rate in horseradish peroxidase as studied by temperature-jump method
    • Morishima, I., Ogawa, S., Yonezawa, T., Nakatani, I. & Hiromi, K. (1978) Unusually fast ligand exchange rate in horseradish peroxidase as studied by temperature-jump method, Biochem. Biophys. Res. Commun. 83, 724-730.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 724-730
    • Morishima, I.1    Ogawa, S.2    Yonezawa, T.3    Nakatani, I.4    Hiromi, K.5
  • 21
    • 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. (1993) 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, 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
  • 22
    • 0025216601 scopus 로고
    • The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin
    • Rohlfs, R. J., Mathews, A. J., Carver, T. E., Olson, J. S., Springer, B. A., Egeberg, K. D. & Sligar, S. G. (1990) The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin, J. Biol. Chem. 265, 3168-3176.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3168-3176
    • Rohlfs, R.J.1    Mathews, A.J.2    Carver, T.E.3    Olson, J.S.4    Springer, B.A.5    Egeberg, K.D.6    Sligar, S.G.7
  • 23
    • 0026062386 scopus 로고
    • Resonance Raman investigation of ferric iron in horse radish peroxidase and its aromatic donor complexes at room and low temperatures
    • Smulevich, G., English, A. M., Mantini, A. R. & Marzocchi, M. P. (1991) Resonance Raman investigation of ferric iron in horse radish peroxidase and its aromatic donor complexes at room and low temperatures, Biochemistry 30, 772-779.
    • (1991) Biochemistry , vol.30 , pp. 772-779
    • Smulevich, G.1    English, A.M.2    Mantini, A.R.3    Marzocchi, M.P.4
  • 25
    • 0015502050 scopus 로고
    • Mechanism of the reactions of cytochrome c. Rate and equilibrium constants for ligand binding to horse heart ferricytochrome c
    • Sutin, N. & Yandell, J. K. (1972) Mechanism of the reactions of cytochrome c. Rate and equilibrium constants for ligand binding to horse heart ferricytochrome c, J. Biol. Chem. 247, 6932-6936.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6932-6936
    • Sutin, N.1    Yandell, J.K.2
  • 26
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale
    • Takano, T. (1977) Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale, J. Mol. Biol. 110, 537-568.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-568
    • Takano, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.