Mössbauer spectroscopy and biophysics

FEB 01, 1971

By bombarding molecules such as hemoglobin and iron–sulfur proteins with low‐energy gamma rays, we can learn about the electron transfer in biochemical reactions.

DOI: 10.1063/1.3022565

Charles E. Johnson

The emission and resonant reabsorption of low‐energy gamma rays in recoilless nuclear transition offers a convenient way to study biochemical reactions. Biological molecules frequently have a transition‐metal atom, such as iron, at the reactive site, and the ${Fe}^{57}$ nucleus is particularly well suited for precise gamma‐ray spectroscopy. By comparing the Mössbauer spectra of two different forms of one of these molecules, for example the oxidized and reduced forms, we learn something about the electron transfer that takes place in biological systems.

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References

1. A. J. F. Boyle, H. E. Hall, Rep. Progr. Phys. 25, 441 (1962).https://doi.org/RPPHAG
2. R. L. Mössbauer, Z. Physik 151, 124 (1958).https://doi.org/ZEPYAA
3. G. Lang, Phys. Lett. 26A, 223 (1968).
4. E. F. Hartree, Ann. Rep. Progr. Chem. 43, 287 (1946).
5. G. Lang, J. Appl. Phys. 38, 915 (1967).https://doi.org/JAPIAU
6. G. Lang, Quart. Rev. Biophys. 3, 1 (1970).https://doi.org/QRBIAK
7. H. Beinert, G. Palmer, Advances in Enzymology 27, 105 (1965).
8. T. H. Moss, D. Petering, G. Palmer, J. Biol. Chem. 244, 6143 (1969).https://doi.org/JBCHA3
9. G. Palmer, Biochem. Biophys. Res. Comm. 27, 315 (1967).https://doi.org/BBRCA9
10. T. Hollacher, F. Solomon, T. Ragland, J. Biol. Chem. 241, 3452 (1966).https://doi.org/JBCHA3
11. R. C. Bray, G. Palmer, H. Beinert, J. Biol. Chem. 239, 2667 (1964).https://doi.org/BICHF3
12. K. K. Rao, R. Cammack, D. O. Hall, C. E. Johnson, Biochem. J. (to be publ.).
13. C. E. Johnson, R. C. Bray, R. Cammack, D. O. Hall, Proc. Nat. Acad. Sci. 63, 1234 (1969).
14. C. E. Johnson, E. Elstner, J. F. Gibson, G. Benfield, M. C. W. Evans, D. O. Hall, Nature 220, 1291 (1968).https://doi.org/NATUAS
15. J. F. Gibson, D. O. Hall, J. H. M. Thomley, F. R. Whatley, Proc. Nat. Acad. Sci. 56, 987 (1966).
16. J. H. M. Thornley, J. F. Gibson, F. R. Whatley, D. O. Hall, Biochem. Biophys. Res. Comm. 24, 6 (1966).https://doi.org/BBRCA9
17. R. Cooke, J. C. M. Tsibris, P. G. Debrunner, R. Tsai, I. C. Gunsalus, H. Frauenfelder, Proc. Nat. Acad. Sci. 59, 1045 (1968).
18. Y. I. Shethna, P. W. Wilson, R. E. Hansen, H. Beinert, Proc. Nat. Acad. Sci. 52, 1263 (1964).
19. G. V. Novikov, L. A. Syrtsova, G. I. Likhtenshtein, V. A. Trukhtanov, V. F. Rachek, V. I. Gol’danskii, Dokl. Akad. Nauk. SSSR 181, 1170 (1968).https://doi.org/DANKAS
20. D. C. Blomstrom, E. Knight, W. D. Phillips, J. F. Weiher, Proc. Nat. Acad. Sci. 51, 1085 (1964).
21. T. H. Moss, A. J. Bearden, R. G. Bartsch, M. A. Cusanovich, A. San Pietro, Biochem. 7, 1591 (1968).
22. J. F. Boas, B. Window, Australian J. Phys. 19, 573 (1966).

More about the authors

Charles E. Johnson, University of Liverpool.