Unravelling the Roles of Integral Polypeptides in Excitation Energy Transfer of Photosynthetic RC-LH1 Supercomplexes

Thwaites, O ORCID: 0009-0001-4094-5290, Christianson, BM, Cowan, AJ ORCID: 0000-0001-9032-3548, Jäckel, F ORCID: 0000-0002-9486-7996, Liu, LN ORCID: 0000-0002-8884-4819 and Gardner, AM ORCID: 0000-0002-2423-8799 (2023) Unravelling the Roles of Integral Polypeptides in Excitation Energy Transfer of Photosynthetic RC-LH1 Supercomplexes Journal of Physical Chemistry B, 127 (33). pp. 7283-7290. ISSN 1520-6106, 1520-5207

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Abstract

Elucidating the photosynthetic processes that occur within the reaction center-light-harvesting 1 (RC-LH1) supercomplexes from purple bacteria is crucial for uncovering the assembly and functional mechanisms of natural photosynthetic systems and underpinning the development of artificial photosynthesis. Here, we examined excitation energy transfer of various RC-LH1 supercomplexes of Rhodobacter sphaeroides using transient absorption spectroscopy, coupled with lifetime density analysis, and studied the roles of the integral transmembrane polypeptides, PufX and PufY, in energy transfer within the RC-LH1 core complex. Our results show that the absence of PufX increases both the LH1 → RC excitation energy transfer lifetime and distribution due to the role of PufX in defining the interaction and orientation of the RC within the LH1 ring. While the absence of PufY leads to the conformational shift of several LH1 subunits toward the RC, it does not result in a marked change in the excitation energy transfer lifetime.

Item Type:	Article
Uncontrolled Keywords:	Rhodobacter sphaeroides, Light-Harvesting Protein Complexes, Photosynthetic Reaction Center Complex Proteins, Peptides, Bacterial Proteins, Photosynthesis, Energy Transfer
Divisions:	Faculty of Health & Life Sciences Faculty of Science & Engineering > School of Physical Sciences Faculty of Health & Life Sciences > Inst. Systems, Molec & Integrative Biology > Inst. Systems, Molec & Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	04 Aug 2023 10:35
Last Modified:	01 Mar 2026 12:32
DOI:	10.1021/acs.jpcb.3c04466
Related Websites:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3172025
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