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Volumn 437, Issue , 2008, Pages 329-345

Characterization of Ligand Migration Mechanisms inside Hemoglobins from the Analysis of Geminate Rebinding Kinetics

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; GLOBULAR PROTEIN; HEMOGLOBIN; LIGAND; SILICA GEL; SILICON DIOXIDE;

EID: 47049084585     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)37017-1     Document Type: Chapter
Times cited : (7)

References (53)
  • 2
    • 22144454624 scopus 로고    scopus 로고
    • Kinetics of proton release after flash photolysis of 1-(2-nitrophenyl)ethyl sulfate (caged sulfate) in aqueous solutions
    • Abbruzzetti S., Sottini S., Viappiani C., and Corrie J.E.T. Kinetics of proton release after flash photolysis of 1-(2-nitrophenyl)ethyl sulfate (caged sulfate) in aqueous solutions. J. Am. Chem. Soc. 127 (2005) 9865-9874
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9865-9874
    • Abbruzzetti, S.1    Sottini, S.2    Viappiani, C.3    Corrie, J.E.T.4
  • 4
    • 0001311681 scopus 로고    scopus 로고
    • Enhanced geminate ligand rebinding upon photo-dissociation of silica gel-embedded myoglobin-CO
    • Abbruzzetti S., Viappiani C., Bruno S., and Mozzarelli A. Enhanced geminate ligand rebinding upon photo-dissociation of silica gel-embedded myoglobin-CO. Chem. Phys. Lett. 346 (2001) 430-436
    • (2001) Chem. Phys. Lett. , vol.346 , pp. 430-436
    • Abbruzzetti, S.1    Viappiani, C.2    Bruno, S.3    Mozzarelli, A.4
  • 5
    • 0024276811 scopus 로고
    • Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin
    • Agmon N. Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin. Biochemistry 27 (1988) 3507-3511
    • (1988) Biochemistry , vol.27 , pp. 3507-3511
    • Agmon, N.1
  • 6
    • 0028350923 scopus 로고
    • The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin
    • Agmon N., Doster W., and Post F. The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin. Biophys. J. 66 (1994) 1612-1622
    • (1994) Biophys. J. , vol.66 , pp. 1612-1622
    • Agmon, N.1    Doster, W.2    Post, F.3
  • 7
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari A., Jones C.M., Henry E.R., Hofrichter J., and Eaton W. The role of solvent viscosity in the dynamics of protein conformational changes. Science 256 (1992) 1796-1798
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.5
  • 10
    • 3843150359 scopus 로고    scopus 로고
    • Method for detecting extended real-time kinetics in nanosecond laser flash photolysis experiments
    • Banderini A., Sottini S., and Viappiani C. Method for detecting extended real-time kinetics in nanosecond laser flash photolysis experiments. Rev. Sci. Instrum. 75 (2004) 2257-2261
    • (2004) Rev. Sci. Instrum. , vol.75 , pp. 2257-2261
    • Banderini, A.1    Sottini, S.2    Viappiani, C.3
  • 12
    • 0642281492 scopus 로고    scopus 로고
    • Methods for the analysis of transient absorbance data
    • Bonneau R., Wirz J., and Zuberbuehler A.D. Methods for the analysis of transient absorbance data. Pure Appl. Chem. 69 (1997) 979-992
    • (1997) Pure Appl. Chem. , vol.69 , pp. 979-992
    • Bonneau, R.1    Wirz, J.2    Zuberbuehler, A.D.3
  • 15
    • 0023640468 scopus 로고
    • Linkage of functional and structural heterogeneity in proteins: Dynamic hole burning in carboxymyoglobin
    • Campbell B.F., Chance M.R., and Friedman J.M. Linkage of functional and structural heterogeneity in proteins: Dynamic hole burning in carboxymyoglobin. Science 238 (1987) 373-376
    • (1987) Science , vol.238 , pp. 373-376
    • Campbell, B.F.1    Chance, M.R.2    Friedman, J.M.3
  • 18
    • 9144236314 scopus 로고    scopus 로고
    • Laser techniques in the study of drug photochemistry
    • Cosa G., and Scaiano J.C. Laser techniques in the study of drug photochemistry. Photochem. Photobiol. 80 (2004) 159-174
    • (2004) Photochem. Photobiol. , vol.80 , pp. 159-174
    • Cosa, G.1    Scaiano, J.C.2
  • 19
    • 0036298976 scopus 로고    scopus 로고
    • Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories
    • Dantsker D., Samuni U., Friedman A.J., Yang M., Ray A., and Friedman J.M. Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories. J. Mol. Biol. 315 (2002) 239-251
    • (2002) J. Mol. Biol. , vol.315 , pp. 239-251
    • Dantsker, D.1    Samuni, U.2    Friedman, A.J.3    Yang, M.4    Ray, A.5    Friedman, J.M.6
  • 20
    • 20144364368 scopus 로고    scopus 로고
    • A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model
    • Dantsker D., Samuni U., Friedman J.M., and Agmon N. A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model. Biochim. Biophys. Acta 1749 (2005) 234-251
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 234-251
    • Dantsker, D.1    Samuni, U.2    Friedman, J.M.3    Agmon, N.4
  • 21
    • 0001194474 scopus 로고
    • Effect of solvent on protein internal dynamics: The kinetics of ligand binding to myoglobin
    • Gregory R.B. (Ed), Dekker, New York
    • Doster W., Kleinert T., Post F., and Settles M. Effect of solvent on protein internal dynamics: The kinetics of ligand binding to myoglobin. In: Gregory R.B. (Ed). "Protein-Solvent Interactions" (1993), Dekker, New York 375
    • (1993) "Protein-Solvent Interactions" , pp. 375
    • Doster, W.1    Kleinert, T.2    Post, F.3    Settles, M.4
  • 23
  • 24
    • 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., Ridsdale A., Wang J., and Friedman J.M. 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 (1997) 14353-14365
    • (1997) Biochemistry , vol.36 , pp. 14353-14365
    • Huang, J.1    Ridsdale, A.2    Wang, J.3    Friedman, J.M.4
  • 25
    • 0016294586 scopus 로고
    • Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobin
    • Iizuka T., Yamamoto H., Kotani M., and Yonetani T. Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobin. Biochim. Biophys. Acta 371 (1974) 126-139
    • (1974) Biochim. Biophys. Acta , vol.371 , pp. 126-139
    • Iizuka, T.1    Yamamoto, H.2    Kotani, M.3    Yonetani, T.4
  • 28
    • 0032512436 scopus 로고    scopus 로고
    • Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin
    • Kleinert T., Doster W., Leyser H., Petry W., Schwarz V., and Settles M. Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin. Biochemistry 37 (1998) 717-733
    • (1998) Biochemistry , vol.37 , pp. 717-733
    • Kleinert, T.1    Doster, W.2    Leyser, H.3    Petry, W.4    Schwarz, V.5    Settles, M.6
  • 29
    • 0041821411 scopus 로고    scopus 로고
    • Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix
    • Kriegl J.M., Forster F.K., and Nienhaus G.U. Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix. Biophys. J. 85 (2003) 1851-1870
    • (2003) Biophys. J. , vol.85 , pp. 1851-1870
    • Kriegl, J.M.1    Forster, F.K.2    Nienhaus, G.U.3
  • 32
    • 0027992932 scopus 로고
    • Ligand binding to heme proteins: The effect of light on ligand binding in myoglobin
    • Nienhaus G.U., Mowant J.R., Chu K., and Frauenfelder H. Ligand binding to heme proteins: The effect of light on ligand binding in myoglobin. Biochemistry 33 (1994) 13413-13430
    • (1994) Biochemistry , vol.33 , pp. 13413-13430
    • Nienhaus, G.U.1    Mowant, J.R.2    Chu, K.3    Frauenfelder, H.4
  • 33
    • 0036040539 scopus 로고    scopus 로고
    • Infrared study of carbon monoxide migration among internal cavities of myoglobin mutant L29W
    • Nienhaus G.U., and Nienhaus K. Infrared study of carbon monoxide migration among internal cavities of myoglobin mutant L29W. J. Biol. Phys. 28 (2002) 163-172
    • (2002) J. Biol. Phys. , vol.28 , pp. 163-172
    • Nienhaus, G.U.1    Nienhaus, K.2
  • 34
    • 0041742184 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Effect of internal cavities on ligand migration and binding
    • Nienhaus K., Deng P., Kriegl J.M., and Nienhaus G.U. Structural dynamics of myoglobin: Effect of internal cavities on ligand migration and binding. Biochemistry 42 (2003) 9647-9658
    • (2003) Biochemistry , vol.42 , pp. 9647-9658
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 35
    • 0042242570 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W
    • Nienhaus K., Deng P., Kriegl J.M., and Nienhaus G.U. Structural dynamics of myoglobin: Spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W. Biochemistry 42 (2003) 9633-9646
    • (2003) Biochemistry , vol.42 , pp. 9633-9646
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 37
    • 7244239027 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels
    • Samuni U., Dantsker D., Juszczak L.J., Bettati S., Ronda L., Mozzarelli A., and Friedman J.M. Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels. Biochemistry 43 (2004) 13674-13682
    • (2004) Biochemistry , vol.43 , pp. 13674-13682
    • Samuni, U.1    Dantsker, D.2    Juszczak, L.J.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6    Friedman, J.M.7
  • 38
    • 0037067708 scopus 로고    scopus 로고
    • Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin
    • Samuni U., Dantsker D., Khan I., Friedman A.J., Peterson E., and Friedman J.M. Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin. J. Biol. Chem. 277 (2002) 25783-25790
    • (2002) J. Biol. Chem. , vol.277 , pp. 25783-25790
    • Samuni, U.1    Dantsker, D.2    Khan, I.3    Friedman, A.J.4    Peterson, E.5    Friedman, J.M.6
  • 40
    • 33644680949 scopus 로고    scopus 로고
    • Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation
    • Samuni U., Roche C.J., Dantsker D., Juszczak L.J., and Friedman J.M. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation. Biochemistry 45 (2006) 2820-2835
    • (2006) Biochemistry , vol.45 , pp. 2820-2835
    • Samuni, U.1    Roche, C.J.2    Dantsker, D.3    Juszczak, L.J.4    Friedman, J.M.5
  • 42
    • 0029163340 scopus 로고
    • Fixation of the quaternary structures of human adult hemoglobin by encapsulation in transparent porous silica gels
    • Shibayama N., and Saigo S. Fixation of the quaternary structures of human adult hemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251 (1995) 203-209
    • (1995) J. Mol. Biol. , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 43
    • 29044440086 scopus 로고    scopus 로고
    • Geminate rebinding in R state hemoglobin: Kinetic and computational evidence for multiple hydrophobic pockets
    • Sottini S., Abbruzzetti S., Spyrakis F., Bettati S., Ronda L., Mozzarelli A., and Viappiani C. Geminate rebinding in R state hemoglobin: Kinetic and computational evidence for multiple hydrophobic pockets. J. Am. Chem. Soc. 127 (2005) 17427-17432
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17427-17432
    • Sottini, S.1    Abbruzzetti, S.2    Spyrakis, F.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6    Viappiani, C.7
  • 44
    • 21644452454 scopus 로고    scopus 로고
    • Evidence for two geminate rebinding states following laser photolysis of R state hemoglobin encapsulated in wet silica gels
    • Sottini S., Abbruzzetti S., Viappiani C., Bettati S., Ronda L., and Mozzarelli A. Evidence for two geminate rebinding states following laser photolysis of R state hemoglobin encapsulated in wet silica gels. J. Phys. Chem. B 109 (2005) 11411-11413
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11411-11413
    • Sottini, S.1    Abbruzzetti, S.2    Viappiani, C.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6
  • 45
    • 27544515467 scopus 로고    scopus 로고
    • Determination of microscopic rate constants for CO binding and migration in myoglobin encapsulated in silica gels
    • Sottini S., Abbruzzetti S., Viappiani C., Ronda L., and Mozzarelli A. Determination of microscopic rate constants for CO binding and migration in myoglobin encapsulated in silica gels. J. Phys. Chem. B 109 (2005) 19523-19528
    • (2005) J. Phys. Chem. B , vol.109 , pp. 19523-19528
    • Sottini, S.1    Abbruzzetti, S.2    Viappiani, C.3    Ronda, L.4    Mozzarelli, A.5
  • 46
    • 3042552036 scopus 로고    scopus 로고
    • CO rebinding kinetics to myoglobin- and R state hemoglobin-doped silica gels in the presence of glycerol
    • Sottini S., Viappiani C., Ronda L., Bettati S., and Mozzarelli A. CO rebinding kinetics to myoglobin- and R state hemoglobin-doped silica gels in the presence of glycerol. J. Phys. Chem. B 108 (2004) 8475-8484
    • (2004) J. Phys. Chem. B , vol.108 , pp. 8475-8484
    • Sottini, S.1    Viappiani, C.2    Ronda, L.3    Bettati, S.4    Mozzarelli, A.5
  • 47
    • 0025845767 scopus 로고
    • Ligand binding to heme proteins: Connection between dynamics and function
    • Steinbach P.J. Ligand binding to heme proteins: Connection between dynamics and function. Biochemistry 30 (1991) 3988-4001
    • (1991) Biochemistry , vol.30 , pp. 3988-4001
    • Steinbach, P.J.1
  • 48
    • 0036863052 scopus 로고    scopus 로고
    • Inferring lifetime distributions from kinetics by maximizing entropy using a bootstrapped model
    • Steinbach P.J. Inferring lifetime distributions from kinetics by maximizing entropy using a bootstrapped model. J. Chem. Inf. Comput. Sci. 42 (2002) 1476-1478
    • (2002) J. Chem. Inf. Comput. Sci. , vol.42 , pp. 1476-1478
    • Steinbach, P.J.1
  • 49
    • 0036212631 scopus 로고    scopus 로고
    • Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: Application to protein folding
    • Steinbach P.J., Ionescu R., and Matthews C.R. Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: Application to protein folding. Biophys. J. 82 (2002) 2244-2255
    • (2002) Biophys. J. , vol.82 , pp. 2244-2255
    • Steinbach, P.J.1    Ionescu, R.2    Matthews, C.R.3
  • 50
    • 0346057931 scopus 로고    scopus 로고
    • Competition with xenon elicits ligand migration and escape pathways in myoglobin
    • Tetreau C., Blouquit Y., Novikov E., Quiniou E., and Lavalette D. Competition with xenon elicits ligand migration and escape pathways in myoglobin. Biophys. J. 86 (2004) 435-447
    • (2004) Biophys. J. , vol.86 , pp. 435-447
    • Tetreau, C.1    Blouquit, Y.2    Novikov, E.3    Quiniou, E.4    Lavalette, D.5
  • 51
    • 23144435806 scopus 로고    scopus 로고
    • Dominant features of protein reaction dynamics: Conformational relaxation and ligand migration
    • Tetreau C., and Lavalette D. Dominant features of protein reaction dynamics: Conformational relaxation and ligand migration. Biochim. Biophys. Acta 1724 (2005) 411-424
    • (2005) Biochim. Biophys. Acta , vol.1724 , pp. 411-424
    • Tetreau, C.1    Lavalette, D.2
  • 52
    • 2642521269 scopus 로고    scopus 로고
    • The structure of murine neuroglobin: Novel pathways for ligand migration and binding
    • Vallone B., Nienhaus K., Matthes K., Brunori M., and Nienhaus G.U. The structure of murine neuroglobin: Novel pathways for ligand migration and binding. Proteins 56 (2004) 85
    • (2004) Proteins , vol.56 , pp. 85
    • Vallone, B.1    Nienhaus, K.2    Matthes, K.3    Brunori, M.4    Nienhaus, G.U.5


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