Probing the topography of the photosystem II oxygen evolving complex: PsbO is required for efficient calcium protection of the manganese cluster against dark-inhibition by an artificial reductant.

Abstract:

:The photosystem II (PSII) manganese-stabilizing protein (PsbO) is known to be the essential PSII extrinsic subunit for stabilization and retention of the Mn and Cl(-) cofactors in the oxygen evolving complex (OEC) of PSII, but its function relative to Ca(2+) is less clear. To obtain a better insight into the relationship, if any, between PsbO and Ca(2+) binding in the OEC, samples with altered PsbO-PSII binding properties were probed for their potential to promote the ability of Ca(2+) to protect the Mn cluster against dark-inhibition by an exogenous artificial reductant, N,N-dimethylhydroxylamine. In the absence of the PsbP and PsbQ extrinsic subunits, Ca(2+) and its surrogates (Sr(2+), Cd(2+)) shield Mn atoms from inhibitory reduction (Kuntzleman et al., Phys Chem Chem Phys 6:4897, 2004). The results presented here show that PsbO exhibits a positive effect on Ca(2+) binding in the OEC by facilitating the ability of the metal to prevent inhibition of activity by the reductant. The data presented here suggest that PsbO may have a role in the formation of the OEC-associated Ca(2+) binding site by promoting the equilibrium between bound and free Ca(2+) that favors the bound metal.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Popelkova H,Boswell N,Yocum C

doi

10.1007/s11120-011-9703-8

subject

Has Abstract

pub_date

2011-12-01 00:00:00

pages

111-21

issue

2

eissn

0166-8595

issn

1573-5079

journal_volume

110

pub_type

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