Crystallographic analysis of the photosynthetic reaction center from Rhodobacter sphaeroides bioconjugated with an artificial antenna. Issue 57 (11th January 2016)

• Record Type: Journal Article
• Authors: Belviso, Benny Danilo; Tangorra, Rocco Roberto; Milano, Francesco; Hassan Omar, Omar; la Gatta, Simona; Ragni, Roberta; Agostiano, Angela; Farinola, Gianluca M.; Caliandro, Rocco; Trotta, Massimo
• Is Part Of: MRS advances. Volume 1:Issue 57(2016)
• Page Start: 3789
• Page End: 3800
• Publication Date: 2016-01-11
• Subjects: macromolecular structure, -- biomimetic (assembly), -- biological synthesis (chemical reaction); Electrical engineering -- Congresses; Physics -- Congresses; Materials -- Research -- Congresses; Materials science -- Congresses; 620.11
• DOI: 10.1557/adv.2016.10
• Languages: English
• ISSNs: 2059-8521

Abstract

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.