Photoaccumulation of membrane preparations of Chlamydomonas reinhardtii at pH 8 and 220 K reduces the primary and secondary electron acceptors in the Photosystem I (PSI) reaction centre, and produces a maximum of two spins per P700(z.rad;+). Proton electron nuclear double resonance (ENDOR) spectra demonstrate that the phyllosemiquinone produced is that attributed to the PsaA branch of electron transfer. Photoaccumulation at pH 10 and 220 K produces a maximum of four spins per P700(z.rad;+), and proton ENDOR spectra indicate that a second phyllosemiquinone is being photoaccumulated, with markedly different proton hyperfine couplings (hfcs). This phyllosemiquinone is unaffected by mutation of PsaAW693, confirming that it does not arise from the PsaA branch of electron transfer, and we therefore attribute it to the PsaB phyllosemiquinone.
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http://dx.doi.org/10.1016/s0005-2728(02)00281-5 | DOI Listing |
Phys Chem Chem Phys
April 2016
Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via Celoria 26, 20133 Milano, Italy.
The oxidation kinetics of phyllo(semi)quinone (PhQ), which acts as an electron transfer (ET) intermediate in the Photosystem I reaction centre, are described by a minimum of two exponential phases, characterised by lifetimes in the 10-30 ns and 150-300 ns ranges. The fastest phase is considered to be dominated by the oxidation of the PhQ molecule coordinated by the PsaB reaction centre subunit (PhQB), and the slowest phase is dominated by the oxidation of the PsaA coordinated PhQ (PhQA). Testing different energetic schemes within a unified theory-based kinetic modelling approach provides reliable limit-values for some of the physical-chemical parameters controlling these ET reactions: (i) the value of ΔG(0) associated with PhQA oxidation is smaller than ∼+30 meV; (ii) the value of the total reorganisation energy (λt) likely exceeds 0.
View Article and Find Full Text PDFBiochim Biophys Acta
August 2014
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA; Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address:
The axial ligands of the acceptor chlorophylls, A(0A) and A(0B), in Photosystem I are the Met sulfur atoms of M688(PsaA) and M668(PsaB). To determine the role of the Met, His variants were generated in Synechocystis sp. PCC 6803.
View Article and Find Full Text PDFJ Phys Chem B
July 2010
Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA.
The kinetics of electron transfer from phyllosemiquinone (PhQ(*-)) to the iron sulfur cluster F(X) in Photosystem I (PS I) are described by lifetimes of approximately 20 and approximately 250 ns. These two rates are attributed to reactions involving the quinones bound primarily by the PsaB (PhQ(B)) and PsaA (PhQ(A)) subunits, respectively. The factors leading to a approximately 10-fold difference between the observed lifetimes are not yet clear.
View Article and Find Full Text PDFBiochemistry
February 2005
School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, United Kingdom.
The spin-correlated radical pair [P(700)(+)A(1)(-)] gives rise to a characteristic "out-of-phase" electron spin-echo signal. The electron spin-echo envelope modulation (ESEEM) of these signals has been studied in thylakoids prepared from the wild-type strain of Chlamydomonas reinhardtii and in two site-directed mutants, in which the methionine residue which acts as the axial ligand to the chlorin electron acceptor A(0) has been substituted with a histidine either on the PsaA (PsaA-M684H) or the PsaB (PsaB-M664H) reaction center subunits. The analysis of the time domain ESEEM provides information about the spin-spin interaction in the [P(700)(+)A(1)(-)] radical pair, and the values of the dipolar (D) and the exchange (J) interaction can be extracted.
View Article and Find Full Text PDFBiochim Biophys Acta
September 2003
School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.
We have used pulsed electron paramagnetic resonance (EPR) measurements of the electron spin polarised (ESP) signals arising from the geminate radical pair P700(z.rad;+)/A(1)(z.rad;-) to detect electron transfer on both the PsaA and PsaB branches of redox cofactors in the photosystem I (PSI) reaction centre of Chlamydomonas reinhardtii.
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