Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-29T10:55:19.986Z Has data issue: false hasContentIssue false

Heme Proteins Encapsulated in Sol-Gel Derived Silica Glasses and their Reaction with Ligands

Published online by Cambridge University Press:  15 February 2011

E. H. Lan
Affiliation:
Department of Material Science and Engineering, University of California at Los Angeles
M. S. Davidson
Affiliation:
Department of Material Science and Engineering, University of California at Los Angeles
L. M. Ellerby
Affiliation:
Department of Chemistry and Biochemistry, University of California at Los Angeles
B. Dunn
Affiliation:
Department of Chemistry and Biochemistry, University of California at Los Angeles
J. Selverstone Valentine
Affiliation:
Department of Chemistry and Biochemistry, University of California at Los Angeles
J. I. Zink
Affiliation:
Department of Chemistry and Biochemistry, University of California at Los Angeles
Get access

Abstract

Hemoglobin (Hb) and myoglobin (Mb) were encapsulated in transparent silica glasses prepared by the sol-gel method. The preparation of the silica glasses was tailored so that when proteins were entrapped in the pores of the inorganic matrix, they retained their biochemical activity, i.e. they could bind ligands reversibly. Using optical spectroscopy to monitor ligand binding, we studied the binding of O2, CO, and NO with these two heme proteins encapsulated in silica glasses and compared them to heme proteins in aqueous buffer. Both Hb and Mb in the sol-gel glass bound O2, CO, and NO, producing the same spectroscopic properties as those in aqueous buffer. In addition, silica encapsulated Mb was used to evaluate the rate of ligand (O2) transport through the pores of the glass. When varying oxygen concentration and measuring the time required for full conversion of deoxyMb to MbO2 in the silica gel, the time vs. concentration data followed an exponential trend, as expected for diffusion controlled processes.

Type
Research Article
Copyright
Copyright © Materials Research Society 1994

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Antonini, E. and Brunori, M., Hemoglobin and Myoglobin in Their Reaction with Ligands.. (North-Holland Publishing Co., Amsterdam, 1971).Google Scholar
2. Dolphin, D., ed., The Porphyrins, Vol. III, (Academic Press, New York, 1978).Google Scholar
3. Ellerby, L. M., Nishida, C. R., Nishida, F., Yamanaka, S. A., Dunn, B., Valentine, J. S., and Zink, J. I., Science 255, 1113 (1992).Google Scholar
4. Yamanaka, S. A., Nishida, F., Ellerby, L. M., Nishida, C. R., Dunn, B., Valentine, J. S., and Zink, J. I., Chem. Mater. 4, 495 (1992).CrossRefGoogle Scholar
5. Avnir, D., Braun, S., and Ottolenghi, M., Supermolecular Architecture in Two and Three Dimensions, Bein, T., ed., ACS Symp. Series 499 (American Chemical Society, New York, 1992).Google Scholar
6. Glezer, V. and Lev, O., J. Am. Chem. Soc. 115,2533 (1993).Google Scholar
7. Audebert, P., Demaille, C., and Sanchez, C., Chem. Mater. 5,911 (1993).CrossRefGoogle Scholar
8. Hench, L. L. and West, J. K., Chem. Rev. 90, 33 (1990).CrossRefGoogle Scholar
9. Brinker, C. J. and Scherer, G., Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing, (Academic Press, New York, 1990).Google Scholar
10. Wittenberg, J. B., Noble, R. W., Wittenberg, B. A., Antonini, E., Brunori, M., and Wyman, J., J. Biol. Chem. 242, 626 (1967).CrossRefGoogle Scholar
11. Chien, J. C., J. Am. Chem. Soc. 91, 2166 (1969).Google Scholar
12. Lougovois, V. and Houston, T. W., Food Chemistry 32, 47 (1989).Google Scholar
13. Wade, R. S. and Castro, C. S., Chem. Res. Toxicol. 3,289 (1990).CrossRefGoogle Scholar
14. Lange's Handbook of Chemistry, Dean, J. A., ed., (McGraw Hill, New York, 1985).Google Scholar