Altered structure of the Mn4Ca cluster in the oxygen-evolving complex of photosystem II by a histidine ligand mutation.

ABSTRACT: The effect of replacing a histidine ligand on the properties of the oxygen-evolving complex (OEC) and the structure of the Mn(4)Ca cluster in Photosystem II (PSII) is studied by x-ray absorption spectroscopy using PSII core complexes from the Synechocystis sp. PCC 6803 D1 polypeptide mutant H332E. In the x-ray crystallographic structures of PSII, D1-His(332) has been assigned as a direct ligand of a manganese ion, and the mutation of this histidine ligand to glutamate has been reported to prevent the advancement of the OEC beyond the S(2)Yz(•) intermediate state. The manganese K-edge (1s core electron to 4p) absorption spectrum of D1-H332E shifts to a lower energy compared with that of the native WT samples, suggesting that the electronic structure of the manganese cluster is affected by t

SUBMITTER: Yano J 

PROVIDER: S-EPMC3059017 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature