Abstract
Binding of carbon monoxide and oxygen to sterically protected heme model compounds (basket-handle porphyrins) was investigated in liquid toluene at temperatures from 180 to 300 K by laser flash photolysis. Only a single exponential rebinding process from the solvent could be seen in the time range of 20 nsec to milliseconds. The fraction of ligands that initially escaped into the solvent decreased when the temperature was lowered, and the Arrhenius plots for the rebinding rate coefficients were found to deviate significantly from linearity. These findings suggest that protected heme model compounds might react according to a double energy-barrier scheme. In contrast, the reaction of an unprotected porphyrin can be described by a single energy barrier.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alberding N., Chan S. S., Eisenstein L., Frauenfelder H., Good D., Gunsalus I. C., Nordlund T. M., Perutz M. F., Reynolds A. H., Sorensen L. B. Binding of carbon monoxide to isolated hemoglobin chains. Biochemistry. 1978 Jan 10;17(1):43–51. doi: 10.1021/bi00594a007. [DOI] [PubMed] [Google Scholar]
- Alberding N., Lavalette D., Austin R. H. Hemerythrin's oxygen-binding reaction studied by laser photolysis. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2307–2309. doi: 10.1073/pnas.78.4.2307. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Campbell B. F., Magde D., Sharma V. S. Geminate recombination of CO in rabbit, opossum, and adult hemoglobins. J Biol Chem. 1985 Mar 10;260(5):2752–2756. [PubMed] [Google Scholar]
- Doster W., Beece D., Bowne S. F., DiIorio E. E., Eisenstein L., Frauenfelder H., Reinisch L., Shyamsunder E., Winterhalter K. H., Yue K. T. Control and pH dependence of ligand binding to heme proteins. Biochemistry. 1982 Sep 28;21(20):4831–4839. doi: 10.1021/bi00263a001. [DOI] [PubMed] [Google Scholar]
- Duddell D. A., Morris R. J., Richards J. T. Nanosecond laser photolysis of aqueous carbon monoxy- and oxyhaemoglobin. Biochim Biophys Acta. 1980 Jan 24;621(1):1–8. doi: 10.1016/0005-2795(80)90056-2. [DOI] [PubMed] [Google Scholar]
- Frauenfelder H., Wolynes P. G. Rate theories and puzzles of hemeprotein kinetics. Science. 1985 Jul 26;229(4711):337–345. doi: 10.1126/science.4012322. [DOI] [PubMed] [Google Scholar]
- Hasinoff B. B., Chishti S. B. Viscosity dependence of the kinetics of the diffusion-controlled reaction of carbon monoxide and myoglobin. Biochemistry. 1982 Aug 31;21(18):4275–4278. doi: 10.1021/bi00261a015. [DOI] [PubMed] [Google Scholar]
- Hasinoff B. B., Chishti S. B. Viscosity dependence of the kinetics of the diffusion-controlled reaction of carbon monoxide with the separated alpha and beta chains of hemoglobin. Biochemistry. 1983 Jan 4;22(1):58–61. doi: 10.1021/bi00270a008. [DOI] [PubMed] [Google Scholar]
- 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]
- Lavalette D., Tetreau C., Mispelter J., Momenteau M., Lhoste J. M. Linear free-energy relationships in binding of oxygen and carbon monoxide with heme model compounds and heme proteins. Eur J Biochem. 1984 Dec 17;145(3):555–565. doi: 10.1111/j.1432-1033.1984.tb08592.x. [DOI] [PubMed] [Google Scholar]
- Morris R. J., Gibson Q. H. The role of diffusion in limiting the rate of ligand binding to hemoglobin. J Biol Chem. 1980 Sep 10;255(17):8050–8053. [PubMed] [Google Scholar]
- Page M. I., Jencks W. P. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1678–1683. doi: 10.1073/pnas.68.8.1678. [DOI] [PMC free article] [PubMed] [Google Scholar]
