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Updated: Jun 10, 2026

In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
Published on: October 10, 2014
The double mutation ΔL6MW241F in PsbO, the photosystem II manganese stabilizing protein, yields insights into the
Hana Popelkova1, Alan Commet, Charles F Yocum
1Department of Molecular, Cellular and Developmental Biology, The University of Michigan, Ann Arbor, MI 48109, USA. popelka@umich.edu
Abstract:
The W241F mutation in spinach manganese-stabilizing protein (PsbO) decreases binding to photosystem II (PSII); its thermostability is increased and reconstituted activity is lower [Wyman et al. (2008) Biochemistry 47, 6490-6498]. The results reported here show that W241F cannot adopt a normal solution structure and fails to reconstitute efficient Cl(-) retention by PSII. An N-terminal truncation of W241F, producing the ΔL6MW241F double mutant that resembles some features of cyanobacterial PsbO, significantly repairs the defects in W241F. Our data suggest that the C-terminal F→W mutation likely evolved in higher plants and green algae in order to preserve proper PsbO folding and PSII binding and assembly, which promotes efficient Cl(-) retention in the oxygen-evolving complex.
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