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Spectral and kinetic evidence for two early electron acceptors in photosystem I
Author(s) -
В. А. Шувалов,
Ed Dolan,
Bacon Ke
Publication year - 1979
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.2.770
Subject(s) - electron paramagnetic resonance , p700 , chemistry , photosystem i , photosynthetic reaction centre , electron acceptor , electron transfer , photochemistry , absorption (acoustics) , absorbance , photosystem ii , sulfur , analytical chemistry (journal) , electron , resonance (particle physics) , electron transport chain , nuclear magnetic resonance , materials science , photosynthesis , atomic physics , physics , biochemistry , chromatography , organic chemistry , quantum mechanics , composite material
Triton-fractionated photosystem-I particles poised at -625 mV, where the two bound iron-sulfur proteins are reduced, have been studied by optical and electron paramagnetic resonance spectroscopies from 293 to 5 K. At 5-9 K, these particles exhibit two decay components with lifetimes of 1.3 and 130 msec in the laser pulse-induced absorption and electron paramagnetic resonance signal changes. Spectral properties of the 130-msec decay component reflect the charge separation between P-700 and some iron-sulfur center having a broad optical absorbance in the 400- to 550-nm region and a previously reported electron paramagnetic resonance signal with g = 1.78, 1.88, and 2.08. Spectral properties of the 1-msec decay component indicate photoinduced charge separation between P-700 and a chlorophyll a dimer having absorption bands at 420, 450, and 700 nm. It is assumed that these two acceptors participate in the electron transfer from P-700(*) to the bound iron-sulfur proteins.

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