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Control and pH dependence of ligand binding to heme proteins
Abstract
The recombination after flash photolysis of dioxygen and carbon monoxide with sperm whale myoglobin (Mb), and separated beta chains of human hemoglobin (beta A) and hemoglobin Zürich (beta ZH), has been studied as a function of pH and temperature from 300 to 60 K. At physiological temperatures, a preequilibrium is established between the ligand molecules in the solvent and in the heme pocket. The ligand in the pocket binds to the heme iron by overcoming a barrier at the heme. The association rate is controlled by this final binding step. The association rate of CO to Mb and beta A is modulated by a single titratable group with a pK at 300 K of 5.7. The binding of CO to beta ZH, in which the distal histidine is replaced by arginine, does not depend on pH. Oxygen recombination is independent of pH in all three proteins. Comparison of the binding of CO at 300 K and at low temperatures shows that pH does not affect the preequilibrium but changes the barrier height at the heme. The pH dependence and the difference between O2 and CO binding can be explained by a charge-dipole interaction between the distal histidine and CO.
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Citations
Cited by
Rebinding and relaxation in the myoglobin pocket
Ansari, A., Berendzen, J., Braunstein, D., Cowen, B. R., Frauenfelder, H., Hong, M. K., Iben, I. E. T., Johnson, J. B., Ormos, P., Sauke, T. B., et al. (1987) · Biophysical Chemistry · doi:10.1016/0301-4622(87)80034-0 · Cited by 356
Self-citationAgmon, N., & Hopfield, J. J. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445988 · Cited by 345
Frauenfelder, H., McMahon, B. H., Austin, R. H., Chu, K., & Groves, J. T. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041614298 · Cited by 340
Self-citationGeminate recombination of carbon monoxide to myoglobin
Henry, E. R., Sommer, J. H., Hofrichter, J., Eaton, W. A., & Gellert, M. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80094-1 · Cited by 268
Ligand recombination to the alpha and beta subunits of human hemoglobin.
Olson, J. S., Rohlfs, R. J., & Gibson, Q. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45147-2 · Cited by 58
Metadata
- Authors
- Doster, W., Beece, D., Bowne, S. F., DiIorio, E. E., Eisenstein, L., Frauenfelder, H., Reinisch, L., Shyamsunder, E., Winterhalter, K. H., & Yue, K. T.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1982-09-28
- Volume
- 21
- Issue
- 20
- Pages
- 4831-4839
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1999136578
- Cited by
- 160
- References
- 0
- FWCI
- 5.45
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Control and pH dependence of ligand binding to heme proteins. https://app.cochat.ai/papers/10.1021/bi00263a001
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- Doster, W., Beece, D., Bowne, S. F., DiIorio, E. E., Eisenstein, L., Frauenfelder, H., Reinisch, L., Shyamsunder, E., Winterhalter, K. H., & Yue, K. T. (1982). Control and pH dependence of ligand binding to heme proteins. Biochemistry. https://doi.org/10.1021/bi00263a001
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