Investigations of the chemical and spectroscopic properties of the Mn-metalloprotein complex responsible for photosynthetic oxygen evolution

John E. Sheats, R. Spruck, T. Babcock, R. Ponticiello, J. Shagam, G. C. Dismukes, B. C. Unni-Nair, R. S. Czernuszewicz, J. A. Smegal, M. Baumgarten, S. Artandi

Research output: Contribution to journalConference articlepeer-review

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 languageAmerican English
Pages (from-to)119-123
Number of pages5
JournalPolymeric Materials Science and Engineering, Proceedings of the ACS Division of Polymeric Materials Science and Engineering
Volume61
StatePublished - 1989
Externally publishedYes
EventProceedings of the ACS Division of Polymeric Materials: Science and Engineering - Miami Beach, FL, USA
Duration: Sep 11 1989Sep 18 1989

ASJC Scopus subject areas

  • Chemical Engineering (miscellaneous)
  • Polymers and Plastics

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