Structural basis of efficient electron transport between photosynthetic membrane proteins and plastocyanin in spinach revealed using nuclear magnetic resonance.

In the photosynthetic light reactions of plants and cyanobacteria, plastocyanin (Pc) plays a crucial role as an electron carrier and shuttle protein between two membrane protein complexes: cytochrome b(6)f (cyt b(6)f) and photosystem I (PSI). The rapid turnover of Pc between cyt b(6)f and PSI enables the efficient use of light energy. In the Pc-cyt b(6)f and Pc-PSI electron transfer complexes, the electron transfer reactions are accomplished within <10(-4) s.

NMR study of repair mechanism of DNA photolyase by FAD-induced paramagnetic relaxation enhancement.

Cyclobutane pyrimidine dimer (CPD) photolyases, which contain FAD as a cofactor, use light to repair CPDs. We performed structural analyses of the catalytic site of the Thermus thermophilus CPD photolyase-DNA complex, using FAD-induced paramagnetic relaxation enhancement (PRE). The distances between the tryptophan residues and the FAD calculated from the PRE agree well with those observed in the x-ray structure (with an error of <3 A).