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

Published online by Cambridge University Press:  11 January 2016

Benny Danilo Belviso ,
Rocco Roberto Tangorra ,
Francesco Milano ,
Omar Hassan Omar ,
Simona la Gatta ,
Roberta Ragni ,
Angela Agostiano ,
Gianluca M. Farinola ,
Rocco Caliandro  and
Massimo Trotta
Benny Danilo Belviso
Affiliation:
Istituto di Cristallografia – Consiglio Nazionale delle Ricerche Via Amendola 122/o, 70125 Bari, Italy
Rocco Roberto Tangorra
Affiliation:
Dipartimento di Chimica, Università degli Studi di Bari “Aldo Moro” Via Orabona 4, 70125 Bari, Italy
Francesco Milano
Affiliation:
Istituto per i Processi Chimico Fisici, Consiglio Nazionale delle Ricerche Via Orabona 4, 70125 Bari, Italy
Omar Hassan Omar
Affiliation:
Istituto di Chimica dei Composti Organometallici, Consiglio Nazionale delle Ricerche Via Orabona 4, 70125 Bari, Italy
Simona la Gatta
Affiliation:
Dipartimento di Chimica, Università degli Studi di Bari “Aldo Moro” Via Orabona 4, 70125 Bari, Italy
Roberta Ragni
Affiliation:
Dipartimento di Chimica, Università degli Studi di Bari “Aldo Moro” Via Orabona 4, 70125 Bari, Italy
Angela Agostiano
Affiliation:
Dipartimento di Chimica, Università degli Studi di Bari “Aldo Moro” Via Orabona 4, 70125 Bari, Italy Istituto per i Processi Chimico Fisici, Consiglio Nazionale delle Ricerche Via Orabona 4, 70125 Bari, Italy
Gianluca M. Farinola
Affiliation:
Dipartimento di Chimica, Università degli Studi di Bari “Aldo Moro” Via Orabona 4, 70125 Bari, Italy
Rocco Caliandro*
Affiliation:
Istituto di Cristallografia – Consiglio Nazionale delle Ricerche Via Amendola 122/o, 70125 Bari, Italy
Massimo Trotta*
Affiliation:
Istituto per i Processi Chimico Fisici, Consiglio Nazionale delle Ricerche Via Orabona 4, 70125 Bari, Italy
*
*rocco.caliandro@ic.cnr.it, massimo.trotta@cnr.it.
*rocco.caliandro@ic.cnr.it, massimo.trotta@cnr.it.
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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.

Keywords

macromolecular structurebiomimetic (assembly)biological synthesis (chemical reaction)
Type
Articles
Information
MRS Advances , Volume 1 , Issue 57: Biomaterials and Soft Materials , 2016 , pp. 3789 - 3800
Copyright
Copyright © Materials Research Society 2016 

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Footnotes

§ Present address: Centre for Biomolecular Science, University of Nottingham, University Park Nottingham, NG7 2RD, UK
# Present address: Mossi & Ghisolfi Group, Strada Ribrocca 11, 15057 Tortona (AL), Italy

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