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The structure and function of the 33 kDa extrinsic protein of Photosystem II: A critical assessment

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Abstract

In this review the structure and function of the 33 kDa protein of Photosystem II is examined. Significant controversies exist concerning the solution secondary structure of the protein, the location of its binding site(s) within Photosystem II, the amino acid residues of the 33 kDa protein required for binding and its stoichiometry within the photosystem. The studies which examine these topics are considered from a critical perspective. A hypothetical model of the folding of the 33 kDa extrinsic protein which is supported by site-specific labeling studies and site-directed mutagenesis experiments is presented. Additionally, the function of the protein within the photosystem is unclear. We present a hypothesis that the 33 kDa protein is involved in maintaining the chloride associated with photosynthetic oxygen evolution in close proximity to the oxygen-evolving site.

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  1. Biochemistry and Molecular Biology Section, Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, 70803, USA

    Terry M. Bricker & Laurie K. Frankel

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  1. Terry M. Bricker
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Bricker, T.M., Frankel, L.K. The structure and function of the 33 kDa extrinsic protein of Photosystem II: A critical assessment. Photosynthesis Research 56, 157–173 (1998). https://doi.org/10.1023/A:1006068615220

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