메뉴 건너뛰기




Volumn 78, Issue 6, 2000, Pages 3227-3239

Multiple geminate ligand recombinations in human hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYHEMOGLOBIN; HEMOGLOBIN;

EID: 0034084357     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76859-7     Document Type: Article
Times cited : (25)

References (63)
  • 2
    • 0015991714 scopus 로고
    • The kinetics of conformational changes in hemoglobin, studied by laser photolysis
    • Alpert, B., R. Banerjee, and L. Lindqvist. 1974. The kinetics of conformational changes in hemoglobin, studied by laser photolysis. Proc. Natl. Acad. Sci. USA. 71:558-562.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 558-562
    • Alpert, B.1    Banerjee, R.2    Lindqvist, L.3
  • 3
    • 0002664392 scopus 로고
    • Transient effects in the nanosecond laser photolysis of carboxyhemoglobin: "Cage" recombination and spectral evolution of the protein
    • Alpert, B., S. El Mohsni, L. Lindqvist, and F. Tfibel. 1979. Transient effects in the nanosecond laser photolysis of carboxyhemoglobin: "cage" recombination and spectral evolution of the protein. Chem. Phys. Lett. 64:11-16.
    • (1979) Chem. Phys. Lett. , vol.64 , pp. 11-16
    • Alpert, B.1    Mohsni, S.E.2    Lindqvist, L.3    Tfibel, F.4
  • 6
    • 0027159782 scopus 로고
    • Photoselection in polarized photolysis experiments on heme proteins
    • Ansari, A., C. M. Jones, E. R. Henry, J. Hofrichter, and W. A. Eaton. 1993. Photoselection in polarized photolysis experiments on heme proteins. Biophys. J. 64:852-868.
    • (1993) Biophys. J. , vol.64 , pp. 852-868
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 7
    • 0027207780 scopus 로고
    • Theory of photoselection by intense light pulses. Influence of reorientational dynamics and chemical kinetics on absorbance measurements
    • Ansari, A., and A. Szabo. 1993. Theory of photoselection by intense light pulses. Influence of reorientational dynamics and chemical kinetics on absorbance measurements. Biophys. J. 64:838-851.
    • (1993) Biophys. J. , vol.64 , pp. 838-851
    • Ansari, A.1    Szabo, A.2
  • 9
    • 0018361151 scopus 로고
    • Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
    • Baldwin, J., and C. Chothia. 1979. Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129:175-220.
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 11
    • 0029999815 scopus 로고    scopus 로고
    • Allosteric intermediates in hemoglobin. 1. Nanosecond time-resolved circular dichroism spectroscopy
    • Björling, S. C., R. A. Goldbeck, S. J. Paquette, S. J. Milder, and D. S. Kliger. 1996. Allosteric intermediates in hemoglobin. 1. Nanosecond time-resolved circular dichroism spectroscopy. Biochemistry. 35: 8619-8627.
    • (1996) Biochemistry , vol.35 , pp. 8619-8627
    • Björling, S.C.1    Goldbeck, R.A.2    Paquette, S.J.3    Milder, S.J.4    Kliger, D.S.5
  • 12
    • 0030031593 scopus 로고    scopus 로고
    • Distal cavity fluctuations in myoglobin: Protein motion and ligand diffusion
    • Carlson, M. L., R. M. Regan, and Q. H. Gibson. 1996. Distal cavity fluctuations in myoglobin: protein motion and ligand diffusion. Biochemistry. 35:1125-1136.
    • (1996) Biochemistry , vol.35 , pp. 1125-1136
    • Carlson, M.L.1    Regan, R.M.2    Gibson, Q.H.3
  • 13
    • 0025243607 scopus 로고
    • Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques
    • Carver, T. E., R. J. Rohlfs, J. S. Olson, Q. H. Gibson, R. S. Blackmore, B. A. Springer, and S. G. Sligar. 1990. Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques. J. Biol. Chem. 265: 20007-20020.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20007-20020
    • Carver, T.E.1    Rohlfs, R.J.2    Olson, J.S.3    Gibson, Q.H.4    Blackmore, R.S.5    Springer, B.A.6    Sligar, S.G.7
  • 14
    • 37049110290 scopus 로고
    • Ultra-fast recombination in nanosecond laser photolysis of carbonylhaemoglobin
    • Duddell, D. A., R. J. Morris, and J. T. Richards. 1979. Ultra-fast recombination in nanosecond laser photolysis of carbonylhaemoglobin. J. Chem. Soc. Chem. Commun. 75-76.
    • (1979) J. Chem. Soc. Chem. Commun. , pp. 75-76
    • Duddell, D.A.1    Morris, R.J.2    Richards, J.T.3
  • 15
    • 0018844132 scopus 로고
    • Nanosecond laser photolysis of aqueous carbon monoxy- and oxyhaemoglobin
    • Duddell, D. A., R. J. Morris, and J. T. Richards. 1980. Nanosecond laser photolysis of aqueous carbon monoxy- and oxyhaemoglobin. Biochim. Biophys. Acta. 621:1-8.
    • (1980) Biochim. Biophys. Acta , vol.621 , pp. 1-8
    • Duddell, D.A.1    Morris, R.J.2    Richards, J.T.3
  • 16
    • 0342999391 scopus 로고    scopus 로고
    • Fast time-resolved magnetic optical rotatory dispersion measurements. 1. Mueller analysis of optical and photoselection-induced artifacts
    • Esquerra, R. M., R. A. Goldbeck, D. B. Kim-Shapiro, and D. S. Kliger. 1998a. Fast time-resolved magnetic optical rotatory dispersion measurements. 1. Mueller analysis of optical and photoselection-induced artifacts. J. Phys. Chem. A. 102:8740-8748.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 8740-8748
    • Esquerra, R.M.1    Goldbeck, R.A.2    Kim-Shapiro, D.B.3    Kliger, D.S.4
  • 17
    • 0032534909 scopus 로고    scopus 로고
    • Spectroscopic evidence for nanosecond protein relaxation after photodissociation of myoglobin-CO
    • Esquerra, R. M., R. A. Goldbeck, D. B. Kim-Shapiro, and D. S. Kliger. 1998b. Spectroscopic evidence for nanosecond protein relaxation after photodissociation of myoglobin-CO. Biochemistry. 37:17527-17536.
    • (1998) Biochemistry , vol.37 , pp. 17527-17536
    • Esquerra, R.M.1    Goldbeck, R.A.2    Kim-Shapiro, D.B.3    Kliger, D.S.4
  • 19
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 20
    • 0021818674 scopus 로고
    • Structure, dynamics, and reactivity in hemoglobin
    • Friedman, J. M. 1985. Structure, dynamics, and reactivity in hemoglobin. Science. 228:1273-1280.
    • (1985) Science , vol.228 , pp. 1273-1280
    • Friedman, J.M.1
  • 21
    • 0028308524 scopus 로고
    • Time-resolved resonance raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin
    • Friedman, J. M. 1994. Time-resolved resonance Raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin. Methods Enzymol. 232:205-231.
    • (1994) Methods Enzymol. , vol.232 , pp. 205-231
    • Friedman, J.M.1
  • 22
    • 0019190726 scopus 로고
    • Transient raman study of co-haemoprotein photolysis: Origin of the quantum yield
    • Friedman, J. M., and K. B. Lyons. 1980. Transient Raman study of CO-haemoprotein photolysis: origin of the quantum yield. Nature. 28: 570-572.
    • (1980) Nature , vol.28 , pp. 570-572
    • Friedman, J.M.1    Lyons, K.B.2
  • 24
    • 0014670514 scopus 로고
    • Preparation and properties of α- and β-chains from human hemoglobin
    • Geraci, G., L. J. Parkhurst, and Q. H. Gibson. 1969. Preparation and properties of α- and β-chains from human hemoglobin. J. Biol. Chem. 17:4664-4667.
    • (1969) J. Biol. Chem. , vol.17 , pp. 4664-4667
    • Geraci, G.1    Parkhurst, L.J.2    Gibson, Q.H.3
  • 26
    • 0027375485 scopus 로고
    • Nanosecond time-resolved absorption and polarization dichroism spectroscopies
    • Goldbeck, R. A., and D. S. Kliger. 1993. Nanosecond time-resolved absorption and polarization dichroism spectroscopies. Methods Enzymol. 226:147-177.
    • (1993) Methods Enzymol. , vol.226 , pp. 147-177
    • Goldbeck, R.A.1    Kliger, D.S.2
  • 27
    • 0029899611 scopus 로고    scopus 로고
    • Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis
    • Goldbeck, R. A., S. J. Paquette, S. C. Björling, and D. S. Kliger. 1996. Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis. Biochemistry. 35:8628-8639.
    • (1996) Biochemistry , vol.35 , pp. 8628-8639
    • Goldbeck, R.A.1    Paquette, S.J.2    Björling, S.C.3    Kliger, D.S.4
  • 28
    • 33747738463 scopus 로고
    • Singular value decomposition and the least squares solutions
    • Golub, G. H., and C. Reinsch. 1970. Singular value decomposition and the least squares solutions. Numer. Math. 14:403-420.
    • (1970) Numer. Math. , vol.14 , pp. 403-420
    • Golub, G.H.1    Reinsch, C.2
  • 29
    • 0043141060 scopus 로고    scopus 로고
    • Nonexponential structural relaxations in proteins
    • Hagen, S. J., and W. A. Eaton. 1996. Nonexponential structural relaxations in proteins. J. Chem. Phys. 104:3395-3398.
    • (1996) J. Chem. Phys. , vol.104 , pp. 3395-3398
    • Hagen, S.J.1    Eaton, W.A.2
  • 30
    • 0030197743 scopus 로고    scopus 로고
    • Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature
    • Hagen, S. J., J. Hofrichter, and W. A. Eaton. 1996. Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature. J. Phys. Chem. 100:12008-12021.
    • (1996) J. Phys. Chem. , vol.100 , pp. 12008-12021
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 31
    • 0026633609 scopus 로고
    • Singular value decomposition: Applications to experimental data
    • Henry, E. R., and J. Hofrichter. 1992. Singular value decomposition: applications to experimental data. Methods Enzymol. 210:129-192.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 32
    • 0030907624 scopus 로고    scopus 로고
    • Can a two-state MWC allosteric model explain hemoglobin kinetics?
    • Henry, E. R., C. M. Jones, J. Hofrichter, and W. A. Eaton. 1997. Can a two-state MWC allosteric model explain hemoglobin kinetics? Biochemistry. 36:6511-6528.
    • (1997) Biochemistry , vol.36 , pp. 6511-6528
    • Henry, E.R.1    Jones, C.M.2    Hofrichter, J.3    Eaton, W.A.4
  • 33
    • 0021111948 scopus 로고
    • Geminate recombination of carbon monoxide to myoglobin
    • Henry, E. R., J. H. Sommer, J. Hofrichter, and W. A. Eaton. 1983. Geminate recombination of carbon monoxide to myoglobin. J. Mol. Biol. 166:443-451.
    • (1983) J. Mol. Biol. , vol.166 , pp. 443-451
    • Henry, E.R.1    Sommer, J.H.2    Hofrichter, J.3    Eaton, W.A.4
  • 34
    • 0022256268 scopus 로고
    • Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: Geminate recombination, conformational changes, and intersubunit communication
    • Hofrichter, J., E. R. Henry, J. H. Sommer, R. Deutsch, M. Ikeda-Saito, T. Yonetani, and W. A. Eaton. 1985. Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry. 24:2667-2679.
    • (1985) Biochemistry , vol.24 , pp. 2667-2679
    • Hofrichter, J.1    Henry, E.R.2    Sommer, J.H.3    Deutsch, R.4    Ikeda-Saito, M.5    Yonetani, T.6    Eaton, W.A.7
  • 36
    • 0001700167 scopus 로고
    • Nanosecond absorption spectroscopy of hemoglobin: Elementary processes in kinetic cooperativity
    • Hofrichter, J., J. H. Sommer, E. R. Henry, and W. A. Eaton. 1983. Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. Proc. Natl. Acad. Sci. USA. 80: 2235-2239.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2235-2239
    • Hofrichter, J.1    Sommer, J.H.2    Henry, E.R.3    Eaton, W.A.4
  • 37
    • 0029818947 scopus 로고    scopus 로고
    • Nanosecond step-scan FTIR spectroscopy of hemoglobin-ligand recombination and protein conformational changes
    • Hu, X. H., H. Frei, and T. G. Spiro. 1996. Nanosecond step-scan FTIR spectroscopy of hemoglobin-ligand recombination and protein conformational changes. Biochemistry. 35:13001-13005.
    • (1996) Biochemistry , vol.35 , pp. 13001-13005
    • Hu, X.H.1    Frei, H.2    Spiro, T.G.3
  • 38
    • 0030671072 scopus 로고    scopus 로고
    • Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: Direct evidence for the functional significance of a hierarchy of dynamical processes
    • Huang, J., A. Ridsdale, J. Wang, and J. M. Friedman. 1997. Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: direct evidence for the functional significance of a hierarchy of dynamical processes. Biochemistry. 36:14353-14365.
    • (1997) Biochemistry , vol.36 , pp. 14353-14365
    • Huang, J.1    Ridsdale, A.2    Wang, J.3    Friedman, J.M.4
  • 39
    • 0028799067 scopus 로고
    • Hemoglobin allostery: Resonance raman spectroscopy of kinetic intermediates
    • Jayaraman, V., K. Rodgers, I. Mukeji, and T. Spiro. 1995. Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science. 269:1843-1848.
    • (1995) Science , vol.269 , pp. 1843-1848
    • Jayaraman, V.1    Rodgers, K.2    Mukeji, I.3    Spiro, T.4
  • 41
    • 0026303359 scopus 로고
    • Rotational diffusion effects on absorbance measurements: Limitations to the magic-angle approach
    • Lewis, J. W., and D. S. Kliger. 1991. Rotational diffusion effects on absorbance measurements: limitations to the magic-angle approach. Photochem. Photobiol. 54:963-968.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 963-968
    • Lewis, J.W.1    Kliger, D.S.2
  • 42
    • 0000277737 scopus 로고
    • Implementation of an optical multichannel analyzer for nanosecond flash photolysis measurements
    • Lewis, J. W., G. G. Yee, and D. S. Kliger. 1987. Implementation of an optical multichannel analyzer for nanosecond flash photolysis measurements. Rev. Sci. Instrum. 58:939-943.
    • (1987) Rev. Sci. Instrum. , vol.58 , pp. 939-943
    • Lewis, J.W.1    Yee, G.G.2    Kliger, D.S.3
  • 43
    • 0024468312 scopus 로고
    • The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin
    • Mathews, A. J., R. J. Rohlfs, J. S. Olson, J. Tame, J. P. Renaud, and K. Nagai. 1989. The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin. J. Biol. Chem. 264: 16573-16583.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16573-16583
    • Mathews, A.J.1    Rohlfs, R.J.2    Olson, J.S.3    Tame, J.4    Renaud, J.P.5    Nagai, K.6
  • 44
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., J. Wyman, and J. P. Changeux. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 45
    • 0024121568 scopus 로고
    • The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin
    • Murray, L. P., J. Hofrichter, E. R. Henry, M. Ikeda-Saito, K. Kitagishi, T. Yonetani, and W. A. Eaton. 1988. The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. Proc. Natl. Acad. Sci. USA. 7:2151-2155.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.7 , pp. 2151-2155
    • Murray, L.P.1    Hofrichter, J.2    Henry, E.R.3    Ikeda-Saito, M.4    Kitagishi, K.5    Yonetani, T.6    Eaton, W.A.7
  • 46
    • 0025390007 scopus 로고
    • Laser pulse shortening to subpicosecond in extracavity dye solutions
    • Nesa, F., M. M. Martin, and Y. H. Meyer. 1990. Laser pulse shortening to subpicosecond in extracavity dye solutions. Opt. Commun. 75:294-300.
    • (1990) Opt. Commun. , vol.75 , pp. 294-300
    • Nesa, F.1    Martin, M.M.2    Meyer, Y.H.3
  • 47
    • 0015218730 scopus 로고
    • The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins
    • Olson, J. S., M. E. Andersen, and Q. H. Gibson. 1971. The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. J. Biol. Chem. 246:5919-5923.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5919-5923
    • Olson, J.S.1    Andersen, M.E.2    Gibson, Q.H.3
  • 48
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • Olson, J. S., and G. N. Phillips, Jr. 1996. Kinetic pathways and barriers for ligand binding to myoglobin. J. Biol. Chem. 271:17593-17596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips, G.N.2
  • 49
    • 0023521335 scopus 로고
    • Ligand recombination to the alpha and beta subunits of human hemoglobin
    • Olson, J. S., R. J. Rohlfs, and Q. H. Gibson. 1987. Ligand recombination to the alpha and beta subunits of human hemoglobin. J. Biol. Chem. 262:12930-12938.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12930-12938
    • Olson, J.S.1    Rohlfs, R.J.2    Gibson, Q.H.3
  • 50
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz, M. F. 1979. Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48:327-386.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 51
    • 0024562782 scopus 로고
    • Myoglobin and haemoglobin: Role of distal residues in reactions with haem ligands
    • Perutz, M. F. 1989. Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands. Trends Biochem. Sci. 14:42-44.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 42-44
    • Perutz, M.F.1
  • 52
    • 0016258287 scopus 로고
    • Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
    • Perutz, M. F., J. E. Ladner, S. R. Simon, and C. Ho. 1974. Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry. 13:2163-2173.
    • (1974) Biochemistry , vol.13 , pp. 2163-2173
    • Perutz, M.F.1    Ladner, J.E.2    Simon, S.R.3    Ho, C.4
  • 53
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance raman study of four beta37 mutants of human hemoglobin A
    • Peterson, E. S., and J. M. Friedman. 1998. A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A. Biochemistry. 37:4346-4357.
    • (1998) Biochemistry , vol.37 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 54
    • 0028228087 scopus 로고
    • Ultrafast measurements of geminate recombination of NO with site-specific mutants of human myoglobin
    • Petrich, J. W., J. C. Lambry, S. Balasubramanian, D. G. Lambright, S. G. Boxer, and J. L. Martin. 1994. Ultrafast measurements of geminate recombination of NO with site-specific mutants of human myoglobin. J. Mol. Biol. 238:437-444.
    • (1994) J. Mol. Biol. , vol.238 , pp. 437-444
    • Petrich, J.W.1    Lambry, J.C.2    Balasubramanian, S.3    Lambright, D.G.4    Boxer, S.G.5    Martin, J.L.6
  • 55
    • 0019154562 scopus 로고
    • Rates of isonitrile binding to the isolated alpha and beta subunits of human hemoglobin
    • Reisberg, P. I., and J. S. Olson. 1980. Rates of isonitrile binding to the isolated alpha and beta subunits of human hemoglobin. J. Biol. Chem. 255:4151-4158.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4151-4158
    • Reisberg, P.I.1    Olson, J.S.2
  • 56
    • 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., A. J. Mathews, T. E. Carver, J. S. Olson, B. A. Springer, K. D. Egeberg, and S. G. Sugar. 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    Sugar, S.G.7
  • 57
    • 0023931433 scopus 로고
    • A comparison of the geminate recombination kinetics of several monomeric heme proteins
    • Rohlfs, R. J., J. S. Olson, and Q. H. Gibson. 1988. A comparison of the geminate recombination kinetics of several monomeric heme proteins. J. Biol. Chem. 263:1803-1813.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1803-1813
    • Rohlfs, R.J.1    Olson, J.S.2    Gibson, Q.H.3
  • 58
    • 0025807792 scopus 로고
    • Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin
    • Smerdon, S. J., G. G. Dodson, A. J. Wilkinson, Q. H. Gibson, R. S. Blackmore, T. E. Carver, and J. S. Olson. 1991. Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin. Biochemistry. 30:6252-6260.
    • (1991) Biochemistry , vol.30 , pp. 6252-6260
    • Smerdon, S.J.1    Dodson, G.G.2    Wilkinson, A.J.3    Gibson, Q.H.4    Blackmore, R.S.5    Carver, T.E.6    Olson, J.S.7
  • 59
    • 0025295712 scopus 로고
    • Probing protein structure and dynamics with resonance raman spectroscopy: Cytochrome c peroxidase and hemoglobin
    • Spiro, T. G., G. Smulevich, and C. Su. 1990. Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin. Biochemistry. 29:4497-4508.
    • (1990) Biochemistry , vol.29 , pp. 4497-4508
    • Spiro, T.G.1    Smulevich, G.2    Su, C.3
  • 61
    • 36849126497 scopus 로고
    • Relationship between absorption intensity and fluorescence lifetime of molecules
    • Strickler, S. J., and R. A. Berg. 1962. Relationship between absorption intensity and fluorescence lifetime of molecules. J. Chem. Phys. 37: 814-822.
    • (1962) J. Chem. Phys. , vol.37 , pp. 814-822
    • Strickler, S.J.1    Berg, R.A.2
  • 62
    • 0016668313 scopus 로고
    • Differences in spectra of α and β chains of hemoglobin between the isolated state and in tetramer
    • Sugita, Y. 1974. Differences in spectra of α and β chains of hemoglobin between the isolated state and in tetramer. J. Biol. Chem. 250: 1251-1256.
    • (1974) J. Biol. Chem. , vol.250 , pp. 1251-1256
    • Sugita, Y.1
  • 63
    • 0004055235 scopus 로고
    • Saunders College Publishers, Philadelphia
    • Yariv, A. 1991. Optical Electronics, 2nd Ed. Saunders College Publishers, Philadelphia. 255.
    • (1991) Optical Electronics, 2nd Ed. , pp. 255
    • Yariv, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.