Recruitment of a foreign quinone into the A1 site of photosystem I. Consecutive forward electron transfer from A0 TO A1 to FX with anthraquinone in the A1 site as studied by transient EPR.
In photosystem I (PS I), phylloquinone (PhQ) acts as a low potential electron acceptor during light-induced electron transfer (ET). The origin of the very low midpoint potential of the quinone is investigated by introducing anthraquinone (AQ) into PS I in the presence and absence of the iron-sulfur clusters. Solvent extraction and reincubation is used to obtain PS I particles containing AQ and the iron-sulfur clusters, whereas incubation of the menB rubA double mutant yields PS I with AQ in the PhQ site but no iron-sulfur clusters. Transient electron paramagnetic resonance spectroscopy is used to investigate the orientation of AQ in the binding site and the ET kinetics. The low temperature spectra suggest that the orientation of AQ in all samples is the same as that of PhQ in native PS I. In PS I containing the iron sulfur clusters, (i) the rate of forward electron transfer from the AQ*- to F(X) is found to be faster than from PhQ*- to F(X), and (ii) the spin polarization patterns provide indirect evidence that the preceding ET step from A0*- to quinone is slower than in the native system. The changes in the kinetics are in accordance with the more negative reduction midpoint potential of AQ. Moreover, a comparison of the spectra in the presence and absence of the iron-sulfur clusters suggests that the midpoint potential of AQ is more negative in the presence of F(X). The electron transfer from the AQ- to F(X) is found to be thermally activated with a lower apparent activation energy than for PhQ in native PS I. The spin polarization patterns show that the triplet character in the initial state of P700)*+AQ*- increases with temperature. This behavior is rationalized in terms of a model involving a distribution of lifetimes/redox potentials for A0 and related competition between charge recombination and forward electron transfer from the radical pair P700*+A0*-.
Pushkar
Yulia N
YN
Institut für Experimentalphysik, Freie Universität Berlin, Arnimallee 14, D-14195 Berlin, Germany.
Karyagina
Irina
I
Stehlik
Dietmar
D
Brown
Sarah
S
van der Est
Art
A
D016880:Anisotropy; D000880:Anthraquinones; D002734:Chlorophyll / Q000737:chemistry*; D000458:Cyanobacteria; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D005288:Ferredoxins / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D007700:Kinetics; D046911:Macromolecular Substances; D008280:Magnetics; D009154:Mutation; D010084:Oxidation-Reduction; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex / Q000737:chemistry*; D010971:Plastoquinone; D011809:Quinones / Q000737:chemistry*; D013053:Spectrophotometry; D046939:Synechocystis / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors; D014466:Ultraviolet Rays
D000880:Anthraquinones; D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D011809:Quinones; D002734:Chlorophyll; D010971:Plastoquinone