Spectral and kinetic evidence for two early electron acceptors in photosystem I
- 1 February 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (2) , 770-773
- https://doi.org/10.1073/pnas.76.2.770
Abstract
Triton-fractionated photosystem-I particles poised at -625 mV, where the 2 bound Fe-S proteins are reduced, were studied by optical and EPR spectroscopies from 293-5.degree. K. At 5-9.degree. K, these particles exhibit 2 decay components with lifetimes of 1.3 and 130 ms in the laser pulse-induced absorption and EPR signal changes. Spectral properties of the 130 ms decay component reflect the charge separation between P-700 and some Fe-S center having a broad optical absorbance in the 400-550 nm region and a previously reported EPR 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 2 acceptors participate in the electron transfer from P-700* to the bound Fe-S proteins.This publication has 14 references indexed in Scilit:
- Electron acceptors associated with P-700 in Triton solubilized Photosystem I particles from spinach chloroplastsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1978
- [Primary photoprocesses in light chloroplast fragments].1976
- Flash photolysis electron spin resonance studies of the electron acceptor species at low temperatures in Photosystem I of spinach subchloroplast particlesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- Light-induced reactions of ferredoxin and P700 at low temperaturesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974
- Further characterization of a Photosystem-II particle isolated from spinach chloroplasts by triton treatment: The reaction-center componentsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974
- Oxidation-Reduction Potentials of Bound Iron-Sulfur Proteins of Photosystem IProceedings of the National Academy of Sciences, 1973
- Evidence for the identity of P430 of Photosystem I and chloroplast-bound iron-sulfur proteinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- The primary electron acceptor of photosystem IBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1973
- [2] Flash kinetic spectrophotometryPublished by Elsevier ,1972
- A New Photosynthetic Pigment, “P430”: Its Possible Role as the Primary Electron Acceptor of Photosystem IProceedings of the National Academy of Sciences, 1971