Coordination sphere and structure of the Mn cluster of the oxygen‐evolving complex in photosynthetic organisms

FEBS Letters

Semin, Boris K¹  Parak, Fritz² 

[1]Biophysics Department, Biological Faculty, Moscow State University, Moscow 119899, Russian Federation

[2]Fakultät für Physik E17, Technische Universität München, 85747 Garching, Germany

关键词: Photosystem II;    Oxygen-evolving complex;    Manganese complex;    Iron;    Binuclear iron protein;   

DOI  :  10.1016/S0014-5793(96)01345-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223–226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences of D1 and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of D1 and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.

【 授权许可】

Unknown