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Science 10 February 1989:
Vol. 243. no. 4892, pp. 789 - 791
DOI: 10.1126/science.2916124
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Articles

Science, Vol 243, Issue 4892, 789-791
Copyright © 1989 by American Association for the Advancement of Science

articles

The manganese site of the photosynthetic water-splitting enzyme

GN George, RC Prince, and SP Cramer

EXXON Research and Engineering Company, Annandale, NJ 08801.

As the originator of the oxygen in our atmosphere, the photosynthetic water-splitting enzyme of chloroplasts is vital for aerobic life on the earth. It has a manganese cluster at its active site, but it is poorly understood at the molecular level. Polarized synchrotron radiation was used to examine the x-ray absorption of manganese in oriented chloroplasts. The manganese site, in the "resting" (S1) state, is an asymmetric cluster, which probably contains four manganese atoms, with interatomic separations of 2.7 and 3.3 angstroms; the vector formed by the 3.3-angstrom manganese pair is oriented perpendicular to the membrane plane. Comparisons with model compounds suggest that the cluster contains bridging oxide or hydroxide ligands connecting the manganese atoms, perhaps with carboxylate bridges connecting the 3.3-angstrom manganese pair.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Where plants make oxygen: a structural model for the photosynthetic oxygen-evolving manganese cluster.
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