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Light-induced structural changes in pigment-protein complexes studied with optical spectroscopy

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Light-induced structural changes in pigment-protein complexes studied with optical spectroscopy

Levenberg, Alexander (2026) Light-induced structural changes in pigment-protein complexes studied with optical spectroscopy. PhD thesis, Concordia University.

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Abstract

ABSTRACT
Light-induced structural changes in pigment-protein complexes studied with optical spectroscopy
High-resolution frequency-domain optical spectroscopy methods such as single-molecule spectroscopy (SMS) and non-photochemical spectral hole burning (NPHB) have been extensively employed to study various amorphous systems including glasses, polymers and proteins, and in particular pigment-protein complexes involved in photosynthesis. In all these systems one can observe, even at cryogenic temperatures, the shifts of the zero-phonon lines. These shifts are attributed to small structural changes in the pigment’s environment that can be represented as switching between the minima of the energy landscape. They are observed directly in single-molecule spectroscopy and are the basis of spectral hole formation in NPHB. Understanding these shifts is important for proper interpretation of NPHB and SMS experiments in the context of photosynthesis research. NPHB also can be used to explore the protein energy landscapes. Joint analysis of the hole growth and recovery data for the same pigment-protein system may allow for determination of the molecular origins of the respective structural changes.
In this thesis I address several topics arising in NPHB experiments on pigment-protein complexes:
• The mismatch between the widths of the distributions of the barrier heights and of the tunneling parameter was explained with the presence of at least two distinct NPHB mechanisms featuring overlapping tunneling parameter distributions that arise due to quite different combinations of barrier heights, widths and the masses of the moving/ tunneling entities.
• The slowdown of NPHB with increased light intensity can be explained with the presence of triplet state(s), though strong solvent deuteration effect likely indicates local heating.
• Differences in NPHB and hole recovery behavior of different pigments in the same protein pocket indicate that pigment molecules themselves likely contribute to the small structural changes behind NPHB. Alternatively, pigment molecules affect the relevant barriers by constraining the movements in their immediate protein environment.
• I also describe successfully building and testing a closed-cycle optical cryosystem that will be used in future experiments exploring protein dynamics as well as energy and charge transfer in pigment protein complexes.

Divisions:Concordia University > Faculty of Arts and Science > Physics
Item Type:Thesis (PhD)
Authors:Levenberg, Alexander
Institution:Concordia University
Degree Name:Ph. D.
Program:Physics
Date:16 February 2026
Thesis Supervisor(s):Zazubovits, Valter
Keywords:pigment-protein complexes, optical spectroscopy, spectral dynamics, photosynthetic complexes, energy transfer, non-photochemical spectral hole burning, NPHB, SMS, Excitation Energy Transfer, EET, 5. Protein Energy Landscapes, Light-Induced Conformational Changes
ID Code:997056
Deposited By: Alexander Levenberg
Deposited On:29 Jun 2026 18:01
Last Modified:29 Jun 2026 18:01

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