title: The manganese site of the photosynthetic water-splitting enzyme.
abstract: 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.
authors.affiliation: EXXON Research and Engineering Company, Annandale, NJ 08801.
authors.forename: G N
authors.initials: GN
authors.lastname: George
authors.forename: R C
authors.initials: RC
authors.lastname: Prince
authors.forename: S P
authors.initials: SP
authors.lastname: Cramer
mesh_terms: D002736:Chloroplasts / Q000648:ultrastructure*; D008345:Manganese; D010315:Particle Accelerators; D010788:Photosynthesis; D011487:Protein Conformation
chemical_list: D008345:Manganese