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- W2089968391 abstract "P700, the primary electron donor of photosystem I, is an asymmetric dimer made of one molecule of chlorophyll a‘ (PA) and one of chlorophyll a (PB) that are bound to the homologous PsaA and PsaB polypeptides. While the carbonyl groups of PA are involved in hydrogen-bonding interactions with several surrounding amino acid side chains and a water molecule, PB does not engage hydrogen bonds with the protein. Notably, the residue Thr A739 is donating a strong hydrogen bond to the 9-keto CO group of PA and the homologous residue Tyr B718 is free from interaction with PB. Light-induced FTIR difference spectroscopy of the photooxidation of P700 has been combined with a site-directed mutagenesis attempt to introduce hydrogen bonds to the carbonyl groups of PB in Synechocystis sp. PCC 6803. The FTIR study of the Y(B718)T mutant provides evidence that the 9-keto CO group of PB and PB+ engages a relatively strong hydrogen-bonding interaction with the surroundings in a significant fraction (40 ± 10%) of the reaction centers. Additional mutations on the two PsaB residues homologous to those involved in the main interactions between the PsaA polypeptide and the 10a-carbomethoxy groups of PA affect only marginally the vibrational frequency of the 10a-ester CO group of PB. The FTIR data on single, double, and triple mutants at these PsaB sites indicate a plasticity of the interactions of the carbonyl groups of PB with the surrounding protein. However, these mutations do not perturb the hydrogen-bonding interactions assumed by the 9-keto and 10a-ester CO groups of PA and PA+ with the protein and have only a limited effect on the relative charge distribution between PA+ and PB+." @default.
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- W2089968391 date "2005-03-09" @default.
- W2089968391 modified "2023-09-25" @default.
- W2089968391 title "Evidence for Hydrogen Bond Formation to the PsaB Chlorophyll of P700 in Photosystem I Mutants of<i>Synechocystis</i>sp. PCC 6803" @default.
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- W2089968391 doi "https://doi.org/10.1021/bi0473612" @default.
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