Berlin 2018 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 15: Postersession III

BP 15.48: Poster

Dienstag, 13. März 2018, 14:00–16:00, Poster B

Analysis of photoinduced processes of the cyanophage-encoded phycobiliprotein Lyase ΦCpeT:PEB using femtosecond transient absorption spectroscopy — •Christopher Carlein, Maximilian Theiß, Natascha Riedel, Nicole Frankenberg-Dinkel, and Rolf Diller — TU Kaiserslautern, 67663 Kaiserslautern, Germany

Phycobiliprotein lyases mediate the chromophore assembly of light harvesting phycobiliproteins in cyanobacteria (1). Interestingly, some cyanophages, viruses that infect cyanobacteria, also possess genes encoding phycobiliprotein lyases. It has been suggested that they might contribute to increasing photosynthetic efficiency in cyanobacteria during infection (2). The cyanophage P-HM1 encoded phycobiliprotein lyase ΦCpeT is forming a stable non-covalent complex with the linear tetrapyrrole phycoerythrobilin (2). To get a better understanding of how the phycobiliprotein lyases might facilitate the phycobiliprotein assembly we study the interaction of ΦCpeT with its chromophore PEB, employing fs transient absorption in the UV/Vis spectral region. This provides insights into the processes after photoexcitation in protein bound linear tetrapyrroles in contrast to their free form (3,4). Additionally, we use binding site mutants of ΦCpeT to study the conformation of PEB within the lyase.

(1) Overkamp et al. (2014) JBC. 289:26691-26707

(2) Gasper et al. (2017) JBC. 292:3089-3098

(3) Dietzek et al. (2011) CPL. 515:163-169

(4) Singer et al. (2016) CPC. 17:1288-1297