A high-throughput crystallographic investigation on several crystals of photosynthetic reaction center covalently bound to an ad-hoc synthesized artificial antenna (AE600) is presented. The investigation did not show a preferential binding site of the antenna molecule AE600 to the reaction center in the solid phase. An accurate crystallographic study allowed identifying a lysine residue sitting on periplasmic side of the protein as one of the bioconjugation sites. The residue sits on subunit M of the protein, in close proximity to the bacteriochlorophylls of the reaction center involved in the light absorption and conversion processes. Distances obtained from the crystallographic structure confirm that energy transfer between the antenna and the protein proceed with the Förster resonance mechanism.

Crystallographic analysis of the photosynthetic reaction center from Rhodobacter sphaeroides bioconjugated with an artificial antenna

TANGORRA, ROCCO ROBERTO;LA GATTA, SIMONA;RAGNI, ROBERTA;AGOSTIANO, Angela;FARINOLA, Gianluca Maria;
2016-01-01

Abstract

A high-throughput crystallographic investigation on several crystals of photosynthetic reaction center covalently bound to an ad-hoc synthesized artificial antenna (AE600) is presented. The investigation did not show a preferential binding site of the antenna molecule AE600 to the reaction center in the solid phase. An accurate crystallographic study allowed identifying a lysine residue sitting on periplasmic side of the protein as one of the bioconjugation sites. The residue sits on subunit M of the protein, in close proximity to the bacteriochlorophylls of the reaction center involved in the light absorption and conversion processes. Distances obtained from the crystallographic structure confirm that energy transfer between the antenna and the protein proceed with the Förster resonance mechanism.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11586/185879
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