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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
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
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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.

Type
Articles
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

References

REFERENCES

Maróti, P. and Trotta, M., in CRC Handbook of Organic Photochemistry and Photobiology, Third Edition - Two Volume Set (CRC Press, 2012), pp. 12891324.CrossRefGoogle Scholar
Dutta, P. K., Lin, S., Loskutov, A., Levenberg, S., Jun, D., Saer, R., Beatty, J. T., Liu, Y., Yan, H. and Woodbury, N. W., J Am Chem Soc 136 (12), 45994604 (2014).CrossRefGoogle Scholar
Dutta, P. K., Levenberg, S., Loskutov, A., Jun, D., Saer, R., Beatty, J. T., Lin, S., Liu, Y., Woodbury, N. W. and Yan, H., J Am Chem Soc 136 (47), 1661816625 (2014).CrossRefGoogle Scholar
Milano, F., Tangorra, R. R., Hassan Omar, O., Ragni, R., Operamolla, A., Agostiano, A., Farinola, G. M. and Trotta, M., Angewandte Chemie 124 (44), 1118111185 (2012).CrossRefGoogle Scholar
Italiano, F., Rinalducci, S., Agostiano, A., Zolla, L., De Leo, F., Ceci, L. R. and Trotta, M., Biometals 25 (5), 939949 (2012).CrossRefGoogle Scholar
Mavelli, F., Trotta, M., Ciriaco, F., Agostiano, A., Giotta, L., Italiano, F. and Milano, F., Eur. Biophys. J., 1-15 (2014).Google Scholar
Ermler, U., Fritzsch, G., Buchanan, S. K. and Michel, H., Structure 2 (10), 925936 (1994).CrossRefGoogle ScholarPubMed
Woodall, A. A., Britton, G. and Jackson, M. J., Bba-Gen Subjects 1336 (3), 575586 (1997).CrossRefGoogle Scholar
Burla, M. C., Caliandro, R., Camalli, M., Carrozzini, B., Cascarano, G. L., De Caro, L., Giacovazzo, C., Polidori, G., Siliqi, D. and Spagna, R., J Appl Crystallogr 40 (3), 609613 (2007).CrossRefGoogle Scholar
Terwilliger, T. C., Grosse-Kunstleve, R. W., Afonine, P. V., Moriarty, N. W., Adams, P. D., Read, R. J., Zwart, P. H. and Hung, L.-W., Acta Crystallographica Section D: Biological Crystallography 64 (5), 515524 (2008).CrossRefGoogle Scholar
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J. and Grosse-Kunstleve, R. W., Acta Crystallographica Section D: Biological Crystallography 66 (2), 213221 (2010).CrossRefGoogle Scholar
Afonine, P. V., Grosse-Kunstleve, R. W. and Adams, P. D., CCP4 Newsl. Protein Crystallogr. 42, contribution 8 (2005).Google Scholar
Chen, V. B., Arendall, W. B. 3rd, Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. and Richardson, D. C., Acta Crystallogr D Biol Crystallogr 66 (Pt 1), 1221 (2010).CrossRefGoogle Scholar
Emsley, P. and Cowtan, K., Acta Crystallogr D Biol Crystallogr 60 (Pt 12 Pt 1), 21262132 (2004).CrossRefGoogle Scholar
Humphrey, W., Dalke, A. and Schulten, K., J Mol Graph Model 14 (1), 3338 (1996).CrossRefGoogle Scholar
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., McNicholas, S. J., Murshudov, G. N., Pannu, N. S., Potterton, E. A., Powell, H. R., Read, R. J., Vagin, A. and Wilson, K. S., Acta Crystallogr D 67, 235242 (2011).CrossRefGoogle Scholar
Caliandro, R. and Belviso, D. B., J Appl Crystallogr 47 (3), 10871096 (2014).CrossRefGoogle Scholar
Clayton, G. M., Peak-Chew, S. Y., Evans, R. M. and Schwabe, J. W., Proc Natl Acad Sci U S A 98 (4), 15491554 (2001).CrossRefGoogle Scholar
Edwards, T. E., Leibly, D. J., Bhandari, J., Statnekov, J. B., Phan, I., Dieterich, S. H., Abendroth, J., Staker, B. L., Van Voorhis, W. C., Myler, P. J. and Stewart, L. J., Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 9), 10321037 (2011).CrossRefGoogle Scholar
Lakowicz, J. R., Principles of Fluorescence Spectroscopy, 3rd edition ed. (Springer, New York, 2006).CrossRefGoogle Scholar