Robustness and Optimality of Light Harvesting in Cyanobacterial Photosystem I
By M. Sener, D. Lu, T. Ritz, Sanghyun Park, P. Fromme, Klaus Schulten. 2002
118 citations recorded by the source corpus.
As most biological species, photosynthetic lifeforms have evolved to function optimally, despite thermal disorder and with fault tolerance. It remains a challenge to understand how this is achieved. To address this challenge, the function of the protein−pigment complex photosystem I (PSI) of the cyanobacterium Synechococcus elongatus is investigated theoretically. The recently obtained high-resolution structure of this complex exhibits an aggregate of 96 chlorophylls that are electronically coupled to function as a light-harvesting antenna complex. This paper constructs an effective Hamiltonian for the chlorophyll aggregate to describe excitation transfer dynamics and spectral properties of PSI. For this purpose, a new kinetic expansion method, the sojourn expansion, is introduced. Our study shows that at room temperature fluctuations of site energies have little effect on the calculated excitation lifetime and quantum yield, which compare favorably with experimental results. The efficiency of the system ...
Subfields: Atomic and Molecular Physics, and Optics, Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5eb7aed72a26e2d94b95b16d0fbecc681c54c705
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In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- Structure and function of photosystems I and II. (2006, background): “Structural information on the geometry of the Chl molecules in PSI permits the construction of microscopic models for an excitation-transfer network of PSI (56, 72, 118, 158, 200, 263, 264, 310).”