Measurement of cofactor distances between P700.+ and A1.- in native and quinone-substituted photosystem I using pulsed electron paramagnetic resonance spectroscopy.
The radical pair P700.+Q.- (P700 = primary electron donor, Q = quinone acceptor) in native photosystem I and in preparations in which the native acceptor (vitamin K1) is replaced by different quinones is investigated by pulsed EPR spectroscopy. In a two-pulse experiment, the light-induced radical pair causes an out-of-phase electron spin echo, showing an envelope modulation. From the modulation frequency, the dipolar coupling, and therefore the distance between the two cofactors, can be derived. The observation of nearly identical distances of about 25.4 A between P700.+ and Q.- in all preparations investigated here leads to the conclusion that the reconstituted quinones are bound to the native A1 binding pocket. Since the orientation of the reconstituted naphthoquinone relative to the axis joining P700.+ and Q*- differs drastically from that of the native vitamin K1, it cannot be bonded to the protein in the same way as the native acceptor. This implies that the function of A1 as an electron acceptor does not depend on the orientation or hydrogen bonding of the quinone.
Zech
S G
SG
Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Germany.
van der Est
A J
AJ
Bittl
R
R
D016227:Benzoquinones / Q000737:chemistry; D000458:Cyanobacteria / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D009285:Naphthoquinones / Q000737:chemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D011809:Quinones / Q000737:chemistry*; D010837:Vitamin K 1 / Q000737:chemistry
D016227:Benzoquinones; D009285:Naphthoquinones; D045322:Photosynthetic Reaction Center Complex Proteins; D011809:Quinones; D010837:Vitamin K 1; C034257:duroquinone