A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii

Alexander Petrenko, Anna Lisa Maniero, Johan Van Tol, Fraser MacMillan, Yajing Li, Louis Claude Brunel, Kevin Redding

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Abstract

High-frequency, high-field EPR at 330 GHz was used to study the photo-oxidized primary donor of photosystem I (P700 +.) in wild-type and mutant forms of photosystem I in the green alga Chlamydomonas reinhardtii. The main focus was the substitution of the axial ligand of the chlorophyll a and chlorophyll a′ molecules that form the P700 heterodimer. Specifically, we examined PsaA-H676Q, in which the histidine axial ligand of the A-side chlorophyll a′ (PA) is replaced with glutamine, and PsaB-H656Q, with a similar replacement of the axial ligand of the B-side chlorophyll a (PB), as well as the double mutant (PsaA-H676Q/PsaB-H656Q), in which both axial ligands were replaced. We also examined the PsaA-T739A mutant, which replaces a threonine residue hydrogen-bonded to the 131-keto group of PA with an alanine residue. The principal g-tensor components of the P700 +. radical determined in these mutants and in wild-type photosystem I were compared with each other, with the monomeric chlorophyll cation radical (Chlz +.) in photosystem II, and with recent theoretical calculations for different model structures of the chlorophyll a+ cation radical. In mutants with a modified PB axial ligand, the gzz component of P700 +. was shifted down by up to 2 × 10-4, while mutations near PA had no significant effect. We discuss the shift of the gzz component in terms of a model with a highly asymmetric distribution of unpaired electron spin in the P700 +. radical cation, mostly localized on PB, and a deviation of the PB chlorophyll structure from planarity due to the axial ligand.

Original languageEnglish (US)
Pages (from-to)1781-1786
Number of pages6
JournalBiochemistry
Volume43
Issue number7
DOIs
StatePublished - Feb 24 2004
Externally publishedYes

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Photosystem I Protein Complex
Chlamydomonas reinhardtii
Paramagnetic resonance
Ligands
Cations
Chlorophyll
Chlorophyta
Photosystem II Protein Complex
Threonine
Algae
Model structures
Glutamine
Histidine
Alanine
Tensors
Hydrogen
Substitution reactions
chlorophyll a
Electrons
Mutation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Petrenko, A., Maniero, A. L., Van Tol, J., MacMillan, F., Li, Y., Brunel, L. C., & Redding, K. (2004). A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii. Biochemistry, 43(7), 1781-1786. https://doi.org/10.1021/bi035466j

A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii. / Petrenko, Alexander; Maniero, Anna Lisa; Van Tol, Johan; MacMillan, Fraser; Li, Yajing; Brunel, Louis Claude; Redding, Kevin.

In: Biochemistry, Vol. 43, No. 7, 24.02.2004, p. 1781-1786.

Research output: Contribution to journalArticle

Petrenko, A, Maniero, AL, Van Tol, J, MacMillan, F, Li, Y, Brunel, LC & Redding, K 2004, 'A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii', Biochemistry, vol. 43, no. 7, pp. 1781-1786. https://doi.org/10.1021/bi035466j
Petrenko A, Maniero AL, Van Tol J, MacMillan F, Li Y, Brunel LC et al. A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii. Biochemistry. 2004 Feb 24;43(7):1781-1786. https://doi.org/10.1021/bi035466j
Petrenko, Alexander ; Maniero, Anna Lisa ; Van Tol, Johan ; MacMillan, Fraser ; Li, Yajing ; Brunel, Louis Claude ; Redding, Kevin. / A High-Field EPR Study of P700 +. in Wild-Type and Mutant Photosystem I from Chlamydomonas reinhardtii. In: Biochemistry. 2004 ; Vol. 43, No. 7. pp. 1781-1786.
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