The protein's role in triplet energy transfer in bacterial reaction centers.

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When photosynthetic organisms are subjected to high-light conditions in nature, electron transfer becomes blocked as the rate of conversion of light into charge-separated states in the reaction center (RC) exceeds the capacity of the soluble carriers involved in cyclic electron transfer. In that event, a well-characterized T{sub 0}-polarized triplet state {sup T}P, is formed on the primary donor, P, from the P{sup +}H{sub A}{sup {minus}} state (reviewed in [1]). In an aerobic or semi-aerobic environment, the major role of the carotenoid (C), also bound by the RC, is to quench {sup T}P prior to its sensitization of the {sup 1}{Delta}{sub ... continued below

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6 p.

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Laible, P. D. August 14, 1998.

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Description

When photosynthetic organisms are subjected to high-light conditions in nature, electron transfer becomes blocked as the rate of conversion of light into charge-separated states in the reaction center (RC) exceeds the capacity of the soluble carriers involved in cyclic electron transfer. In that event, a well-characterized T{sub 0}-polarized triplet state {sup T}P, is formed on the primary donor, P, from the P{sup +}H{sub A}{sup {minus}} state (reviewed in [1]). In an aerobic or semi-aerobic environment, the major role of the carotenoid (C), also bound by the RC, is to quench {sup T}P prior to its sensitization of the {sup 1}{Delta}{sub g} singlet state of oxygen--a potentially damaging biological oxidant. The carotenoid performs this function efficiently in most bacterial RCs by rapidly accepting the triplet state from P and dissipating this excited-state energy into heat through internal conversion. The lowest-lying triplet states of P and the carotenoid are sufficiently different that {sup T}P can promote oxygen to its excited singlet state whereas {sup T}C can quench the {sup T}P state (reviewed in [2]).

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6 p.

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OSTI as DE00010857

Medium: P; Size: 6 pages

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  • 11th International Congress on Photosynthesis, Budapest (HU), 08/17/1998--08/22/1998

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  • Report No.: ANL/CMB/CP-96702
  • Grant Number: W-31109-ENG-38
  • Office of Scientific & Technical Information Report Number: 10857
  • Archival Resource Key: ark:/67531/metadc623599

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  • August 14, 1998

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  • June 16, 2015, 7:43 a.m.

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  • April 11, 2017, 1:25 p.m.

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Laible, P. D. The protein's role in triplet energy transfer in bacterial reaction centers., article, August 14, 1998; Illinois. (digital.library.unt.edu/ark:/67531/metadc623599/: accessed September 19, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.