Protein interactions and electron transfer between cytochrome f and plastocyanin from the cyanobacterium Prochlorothrix hollandica

BIOL 149

Maria V Baranova, bmaria@bgnet.bgsu.edu and George S Bullerjahn, bullerj@bgnet.bgsu.edu. Center for Photochemical Sciences, Bowling Green State University, Bowling Green, OH 43402
Cytochrome f (cytf) and plastocyanin (PC) interact as an electron donor/acceptor pair in all photosynthetic organisms including cyanobacteria during oxygenic photosynthesis. In previous studies, PC from cyanobacteria was shown to interact with cytf differently than in higher plants and algae1. In order to study in vitro interaction between the physiological partners PC and cytf from the cyanobacterium P.hollandica, a novel cytf expression system was developed. P. hollandica is a divergent cyanobacterium exhibiting unique variants of PC and cytf. Recombinant cytf was characterized by MALDI-TOF, UV-Vis, and CD spectroscopy. Midpoint redox potential was determined to be +320 mV. Electron transfer studies revealed that the of unique protuberant amino acids (Tyr and Pro) on the docking surface of PC is rewuired for maximal electron transfer rates. Transient complex formation and structural of the PC/cytf interaction are currently being investigated by 1H-15N HSQC NMR spectroscopy.

1. Schlarb-Ridley B.G.; Bendall D.S.; Howe C.J. Biochemistry 2003, 42, 4057-4063