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. 1993 Oct;65(4):1660–1665. doi: 10.1016/S0006-3495(93)81223-2

A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale.

C L Norris 1, K S Peters 1
PMCID: PMC1225892  PMID: 8274654

Abstract

The development of a photoacoustic calorimeter with a time resolution of 10 ns is presented, and the dynamics of the enthalpy and volume changes found in the photodissociation of CO from horse carboxymyoglobin are examined. With this enhanced time resolution a new transient species, the lifetime of which is 29 ns at 20 degrees C, is observed in the ligand dissociation process.

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Selected References

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  1. Ansari A., Jones C. M., Henry E. R., Hofrichter J., Eaton W. A. The role of solvent viscosity in the dynamics of protein conformational changes. Science. 1992 Jun 26;256(5065):1796–1798. doi: 10.1126/science.1615323. [DOI] [PubMed] [Google Scholar]
  2. Austin R. H., Beeson K. W., Eisenstein L., Frauenfelder H., Gunsalus I. C. Dynamics of ligand binding to myoglobin. Biochemistry. 1975 Dec 2;14(24):5355–5373. doi: 10.1021/bi00695a021. [DOI] [PubMed] [Google Scholar]
  3. Beece D., Eisenstein L., Frauenfelder H., Good D., Marden M. C., Reinisch L., Reynolds A. H., Sorensen L. B., Yue K. T. Solvent viscosity and protein dynamics. Biochemistry. 1980 Nov 11;19(23):5147–5157. doi: 10.1021/bi00564a001. [DOI] [PubMed] [Google Scholar]
  4. Bolognesi M., Cannillo E., Ascenzi P., Giacometti G. M., Merli A., Brunori M. Reactivity of ferric Aplysia and sperm whale myoglobins towards imidazole. X-ray and binding study. J Mol Biol. 1982 Jun 25;158(2):305–315. doi: 10.1016/0022-2836(82)90435-1. [DOI] [PubMed] [Google Scholar]
  5. Case D. A., Karplus M. Dynamics of ligand binding to heme proteins. J Mol Biol. 1979 Aug 15;132(3):343–368. doi: 10.1016/0022-2836(79)90265-1. [DOI] [PubMed] [Google Scholar]
  6. Genberg L., Richard L., McLendon G., Miller R. J. Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales. Science. 1991 Mar 1;251(4997):1051–1054. doi: 10.1126/science.1998121. [DOI] [PubMed] [Google Scholar]
  7. Henry E. R., Sommer J. H., Hofrichter J., Eaton W. A. Geminate recombination of carbon monoxide to myoglobin. J Mol Biol. 1983 May 25;166(3):443–451. doi: 10.1016/s0022-2836(83)80094-1. [DOI] [PubMed] [Google Scholar]
  8. Johnson C. R., Gill S. J., Peters K. S. Thin-layer microcalorimetric studies of oxygen and carbon monoxide binding to hemoglobin and myoglobin. Biophys Chem. 1992 Nov;45(1):7–15. doi: 10.1016/0301-4622(92)87018-e. [DOI] [PubMed] [Google Scholar]
  9. Kuriyan J., Wilz S., Karplus M., Petsko G. A. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. J Mol Biol. 1986 Nov 5;192(1):133–154. doi: 10.1016/0022-2836(86)90470-5. [DOI] [PubMed] [Google Scholar]
  10. Morikis D., Champion P. M., Springer B. A., Sligar S. G. Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry. 1989 May 30;28(11):4791–4800. doi: 10.1021/bi00437a041. [DOI] [PubMed] [Google Scholar]
  11. Peters K. S., Snyder G. J. Time-resolved photoacoustic calorimetry: probing the energetics and dynamics of fast chemical and biochemical reactions. Science. 1988 Aug 26;241(4869):1053–1057. doi: 10.1126/science.3045967. [DOI] [PubMed] [Google Scholar]
  12. Peters K. S., Watson T., Marr K. Time-resolved photoacoustic calorimetry: a study of myoglobin and rhodopsin. Annu Rev Biophys Biophys Chem. 1991;20:343–362. doi: 10.1146/annurev.bb.20.060191.002015. [DOI] [PubMed] [Google Scholar]
  13. Richard L., Genberg L., Deak J., Chiu H. L., Miller R. J. Picosecond phase grating spectroscopy of hemoglobin and myoglobin: energetics and dynamics of global protein motion. Biochemistry. 1992 Nov 10;31(44):10703–10715. doi: 10.1021/bi00159a010. [DOI] [PubMed] [Google Scholar]
  14. Small J. R., Libertini L. J., Small E. W. Analysis of photoacoustic waveforms using the nonlinear least squares method. Biophys Chem. 1992 Jan;42(1):29–48. doi: 10.1016/0301-4622(92)80005-p. [DOI] [PubMed] [Google Scholar]
  15. Takano T. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. J Mol Biol. 1977 Mar 5;110(3):569–584. doi: 10.1016/s0022-2836(77)80112-5. [DOI] [PubMed] [Google Scholar]
  16. Tian WD, Sage JT, Srajer V, V, Champion PM. Relaxation dynamics of myoglobin in solution. Phys Rev Lett. 1992 Jan 20;68(3):408–411. doi: 10.1103/PhysRevLett.68.408. [DOI] [PubMed] [Google Scholar]
  17. Westrick J. A., Goodman J. L., Peters K. S. A time-resolved photoacoustic calorimetry study of the dynamics of enthalpy and volume changes produced in the photodissociation of carbon monoxide from sperm whale carboxymyoglobin. Biochemistry. 1987 Dec 15;26(25):8313–8318. doi: 10.1021/bi00399a043. [DOI] [PubMed] [Google Scholar]
  18. Westrick J. A., Peters K. S. A photoacoustic calorimetric study of horse myoglobin. Biophys Chem. 1990 Aug 31;37(1-3):73–79. doi: 10.1016/0301-4622(90)88008-g. [DOI] [PubMed] [Google Scholar]
  19. Westrick J. A., Peters K. S., Ropp J. D., Sligar S. G. Role of the arginine-45 salt bridge in ligand dissociation from sperm whale carboxymyoglobin as probed by photoacoustic calorimetry. Biochemistry. 1990 Jul 17;29(28):6741–6746. doi: 10.1021/bi00480a026. [DOI] [PubMed] [Google Scholar]

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