Abstract
This work has shown that binuclear and higher manganese clusters can bind water molecules reversibly and deprotonate them to form oxo bridges. Successively higher oxidation states may be stabilized by additional oxo-bridges. One can speculate that when the capacity for oxidation of the cluster is exceeded, oxygen is evolved and the whole process can begin again. This almost certainly is what is happening in the Mn-enzyme.
| Original language | English |
|---|---|
| Title of host publication | Polymeric Materials Science and Engineering, Proceedings of the ACS Division of Polymeric Materials Science and Engineering |
| Publisher | Publ by ACS |
| Pages | 119-123 |
| Number of pages | 5 |
| Volume | 61 |
| Publication status | Published - 1989 |
| Event | Proceedings of the ACS Division of Polymeric Materials: Science and Engineering - Miami Beach, FL, USA Duration: Sep 11 1989 → Sep 18 1989 |
Other
| Other | Proceedings of the ACS Division of Polymeric Materials: Science and Engineering |
|---|---|
| City | Miami Beach, FL, USA |
| Period | 9/11/89 → 9/18/89 |
ASJC Scopus subject areas
- Chemical Engineering (miscellaneous)
- Polymers and Plastics
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Cite this
Sheats, J. E., Spruck, R., Babcock, T., Ponticiello, R., Shagam, J., Dismukes, G. C., Unni-Nair, B. C., Czernuszewicz, R. S., Smegal, J. A., Baumgarten, M., & Artandi, S. (1989). Investigations of the chemical and spectroscopic properties of the Mn-metalloprotein complex responsible for photosynthetic oxygen evolution. In Polymeric Materials Science and Engineering, Proceedings of the ACS Division of Polymeric Materials Science and Engineering (Vol. 61, pp. 119-123). Publ by ACS.