Complex nonexponential relaxation in myoglobin after photodissociation of MbCO: measurement and analysis from 2 ps to 56 υs

[1]  W. Doster,et al.  Structural relaxation and nonexponential kinetics of CO-binding to horse myoglobin. Multiple flash photolysis experiments. , 1993, Biophysical journal.

[2]  C. M. Jones,et al.  The role of solvent viscosity in the dynamics of protein conformational changes. , 1992, Science.

[3]  Champion,et al.  Relaxation dynamics of myoglobin in solution. , 1992, Physical review letters.

[4]  M. D. Chavez,et al.  Evidence for proximal control of ligand specificity in hemeproteins: Absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins☆ , 1991 .

[5]  S. Boxer,et al.  Protein relaxation dynamics in human myoglobin , 1991 .

[6]  V. Šrajer,et al.  Investigations of optical line shapes and kinetic hole burning in myoglobin. , 1991, Biochemistry.

[7]  J. B. Johnson,et al.  Ligand binding to heme proteins: connection between dynamics and function. , 1991, Biochemistry.

[8]  J. Simon,et al.  Protein conformational relaxation following photodissociation of CO from carbonmonoxymyoglobin: picosecond circular dichroism and absorption studies. , 1991, Biochemistry.

[9]  R. Miller,et al.  Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales. , 1991, Science.

[10]  M. Leone,et al.  Thermal behavior of the 760-nm absorption band in photodissociated sperm whale carbonmonoxymyoglobin at cryogenic temperature: dependence on external medium. , 1990, Biopolymers.

[11]  M. Leone,et al.  Structural and dynamic properties of the heme pocket in myoglobin probed by optical spectroscopy , 1988, Biopolymers.

[12]  N Agmon,et al.  Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin. , 1988, Biochemistry.

[13]  J. Kafka,et al.  Peak power fluctuations in optical pulse compression , 1988 .

[14]  M R Chance,et al.  Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin. , 1987, Science.

[15]  D. Rousseau,et al.  Time dependence of near-infrared spectra of photodissociated hemoglobin and myoglobin. , 1987, Biochemistry.

[16]  M Karplus,et al.  X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. , 1986, Journal of molecular biology.

[17]  J. O. Alben,et al.  Structures of photolyzed carboxymyoglobin. , 1985, Biochemistry.

[18]  J. Friedman,et al.  Picosecond time-resolved Raman studies of photodissociated carboxymyoglobin , 1985 .

[19]  R. Palmer,et al.  Models of hierarchically constrained dynamics for glassy relaxation , 1984 .

[20]  S. Phillips,et al.  Structure and refinement of oxymyoglobin at 1.6 A resolution. , 1980, Journal of molecular biology.

[21]  K. Nagai,et al.  Assignment of the Fe—Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin , 1979 .

[22]  T. Takano,et al.  Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. , 1977, Journal of molecular biology.

[23]  T. Takano.  Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. , 1976, Journal of molecular biology.

[24]  T. Yonetani,et al.  Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin. , 1974, Biochimica et biophysica acta.

[25]  Michael F. Shlesinger,et al.  Time‐Scale Invariance in Transport and Relaxation , 1991 .

[26]  J. Hofrichter,et al.  Polarized absorption and linear dichroism spectroscopy of hemoglobin. , 1981, Methods in enzymology.