Role of disulfide linkage and putative intermolecular binding residues in the stability and binding of the extrinsic manganese-stabilizing protein to the photosystem II reaction center

R. L. Burnap, Ming Qian, Jian-Ren Shen, Yorinao Inoue, Louis A. Sherman

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Abstract

Site-directed mutations were produced at three highly conserved amino acid positions of MSP of the photosystem II (PSII) reaction center in the transformable cyanobacterium Synechocystis sp. PCC6803. The highly conserved aspartate at position 9 of the mature MSP was changed to a lysine (strain MSP-D9K) to assess its role in the proposed N-terminal binding region (Eaton-Rye & Murata, 1989; Odom & Bricker, 1992). This strain accumulates normal levels of MSP, and the properties of the H2O-splitting enzyme are only slightly altered relative to the wild-type. In contrast, replacement of cysteine 20 with a serine, which is proposed to disrupt the intramolecular disulfide bridge (Tanaka et al., 1989), produces a phenotype with no detectable accumulation of MSP, despite normal levels of mRNA transcripts. Like the psbO deletion strain, the MSP-C20S mutant exhibits impaired O2 evolution activity and a greater stability of the S2 state as measured by thermoluminescence. Mutation of strictly conserved aspartate 159 to asparagine (MSP-D159N) does not affect the accumulation of MSP, but causes a reduction in the H2O-oxidation activity and thermoluminescence properties intermediate between the wild-type and the psbO deletion strain. In addition, we report upon improved methods for obtaining oxygen-evolving membranes from mutant cells.

Original languageEnglish
Pages (from-to)13712-13718
Number of pages7
JournalBiochemistry
Volume33
Issue number46
Publication statusPublished - 1994
Externally publishedYes

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Photosystem II Protein Complex
Manganese
Aspartic Acid
Disulfides
Synechocystis
Mutation
Thermoluminescence
Asparagine
Cyanobacteria
Serine
Lysine
Cysteine
Proteins
Cell Membrane
Oxygen
Phenotype
Amino Acids
Messenger RNA
Enzymes
Thermodynamic properties

ASJC Scopus subject areas

  • Biochemistry

Cite this

Role of disulfide linkage and putative intermolecular binding residues in the stability and binding of the extrinsic manganese-stabilizing protein to the photosystem II reaction center. / Burnap, R. L.; Qian, Ming; Shen, Jian-Ren; Inoue, Yorinao; Sherman, Louis A.

In: Biochemistry, Vol. 33, No. 46, 1994, p. 13712-13718.

Research output: Contribution to journalArticle

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AU - Qian, Ming

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AU - Inoue, Yorinao

AU - Sherman, Louis A.

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