Light-induced alteration of low-temperature interprotein electron transfer between photosystem I and flavodoxin |
| |
Authors: | Utschig Lisa M Tiede David M Poluektov Oleg G |
| |
Institution: | Chemical Sciences and Engineering Division, Argonne National Laboratory, Argonne, Illinois 60439, United States. utschig@anl.gov |
| |
Abstract: | Electron paramagnetic resonance (EPR) was used to study light-induced electron transfer in Photosystem I-flavodoxin complexes. Deuteration of flavodoxin enables the signals of the reduced flavin acceptor and oxidized primary donor, P(700)(+), to be well-resolved at X- and D-band EPR. In dark-adapted samples, photoinitiated interprotein electron transfer does not occur at 5 K. However, for samples prepared in dim light, significant interprotein electron transfer occurs at 5 K and a concomitant loss of the spin-correlated radical pair P(+)A(1A)(-) signal is observed. These results indicate a light-induced reorientation of flavodoxin in the PSI docking site that allows a high quantum yield efficiency for the interprotein electron transfer reaction. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|