Tuning by Hydrogen Bonding in Photosynthesis.
Kõu TimpmannMargus RätsepErko JalvisteArvi FreibergPublished in: The journal of physical chemistry. B (2024)
Hydrogen bonding plays a crucial role in stabilizing proteins throughout their folding process. In photosynthetic light-harvesting chromoproteins, enriched with pigment chromophores, hydrogen bonds also fine-tune optical absorption to align with the solar irradiation spectrum. Despite its significance for photosynthesis, the precise mechanism of spectral tuning through hydrogen bonding remains inadequately understood. This study investigates wild-type and genetically engineered LH2 and LH1 light-harvesting complexes from Rhodobacter sphaeroides using a unique set of advanced spectroscopic techniques combined with simple exciton modeling. Our findings reveal an intricate interplay between exciton and site energy shift mechanisms, challenging the prevailing belief that spectral changes observed in these complexes upon the modification of tertiary structure hydrogen bonds almost directly follow shifting site energies. These deeper insights into natural adaptation processes hold great promise for advancing sustainable solar energy conversion technologies.
Keyphrases
- energy transfer
- wild type
- optical coherence tomography
- molecular docking
- high resolution
- genome wide
- single molecule
- density functional theory
- dual energy
- single cell
- quantum dots
- big data
- molecular dynamics simulations
- magnetic resonance imaging
- dna methylation
- mass spectrometry
- machine learning
- radiation therapy
- radiation induced