Is the manganese stabilizing 33 kDa protein of photosystem II attaining a ‘natively unfolded’ or ‘molten globule’ structure in solution?

FEBS Letters

Shutova, T.²  Renger, G.²  Irrgang, K.-D.²  Klimov, V.V.¹ 

[1] Institute of Basic Biological Problems, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia;Max-Volmer-Institute for Biophysical Chemistry and Biochemistry, Technical University Berlin, Straße des 17. Juni 135, D-10623 Berlin, Germany

关键词: Manganese stabilizing protein;    Photosystem II;    Water oxidation;    ‘Molten globule’ structure;    CP47;    chlorophyll containing 47 kDa protein;    QA amd QB;    primary and secondary quinone acceptor;    respectively;    of PS II;    MSP;    manganese stabilizing protein;    NACP;    non-Aβ component of Alzheimer's disease amyloid plaque;    precursor;    P680;    redox active chlorophyll-a of PS II;    Pheo;    pheophytin;    PKI;    protein kinase inhibitor;    PS II;    photosystem II;    R S;    Stokes radius;    S e;    sedimentation coefficient;    WOC;    water oxidizing complex;    YZ;    redox active tyrosine of polypeptide D1;   

DOI  :  10.1016/S0014-5793(00)01115-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This study compares the properties of the extrinsic 33 kDa subunit acting as ‘manganese stabilizing protein’ (MSP) of the water oxidizing complex with characteristic features of proteins that are known to attain a ‘natively unfolded’ or a ‘molten globule’ structure. The analysis leads to the conclusion that the MSP in solution is most likely a ‘molten globule’ with well defined compact regions of β structure. The possible role of these structural peculiarities of MSP in solution for its function as important constituent of the WOC is discussed.

【 授权许可】

Unknown