Antagonistic Effects of Point Mutations on Charge Recombination and a New View of Primary Charge Separation in Photosynthetic Proteins

K Dubas, S Szewczyk*, R Białek, G Burdziński, M R Jones, K Gibasiewicz

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

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Light-induced electron-transfer reactions were investigated in wild-type and three mutant Rhodobacter sphaeroides reaction centers with the secondary electron acceptor (ubiquinone QA) either removed or permanently reduced. Under such conditions, charge separation between the primary electron donor (bacteriochlorophyll dimer, P) and the electron acceptor (bacteriopheophytin, HA) was followed by P+HA- → PHA charge recombination. Two reaction centers were used that had different single amino-acid mutations that brought about either a 3-fold acceleration in charge recombination compared to that in the wild-type protein, or a 3-fold deceleration. In a third mutant in which the two single amino-acid mutations were combined, charge recombination was similar to that in the wild type. In all cases, data from transient absorption measurements were analyzed using similar models. The modeling included the energetic relaxation of the charge-separated states caused by protein dynamics and evidenced the appearance of an intermediate charge-separated state, P+BA-, with BA being the bacteriochlorophyll located between P and HA. In all cases, mixing of the states P+BA- and P+HA- was observed and explained in terms of electron delocalization over BA and HA. This delocalization, together with picosecond protein relaxation, underlies a new view of primary charge separation in photosynthesis.

Original languageEnglish
Pages (from-to)8742-8756
Number of pages15
JournalJournal of Physical Chemistry B
Issue number31
Early online date30 Jul 2021
Publication statusPublished - 12 Aug 2021

Bibliographical note

Funding Information:
The studies were financially supported through the project no. 2017/25/N/NZ1/02382 to K.D., funded by The National Science Center (NCN).

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© 2021 American Chemical Society. All rights reserved.

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