A picosecond circular dichroism study of photosynthetic reaction centers from Rhodobacter sphaeroides.
Picosecond transient circular dichroism spectra are reported for the primary intermediates in the photocycle of reaction centers isolated from Rhodobacter sphaeroides. The time-resolved circular dichroism spectra of the two electron transfer intermediates (BChl2) +BPh-LQA and (BChl2) +BPhLQ-A reveal a large, nonconservative, and fairly stationary CD band at 800 nm. These results suggests that mechanisms other than exciton interactions need to be included in order to explain the optical activity of this biological system.
Xie
X L
XL
Department of Chemistry, University of California, San Diego, La Jolla 92093.
Simon
J D
JD
D002942:Circular Dichroism; D004579:Electron Transport; D045322:Photosynthetic Reaction Center Complex Proteins; D012242:Rhodobacter sphaeroides
D045322:Photosynthetic Reaction Center Complex Proteins