Basic Research Needs for Solar Energy Utilization - Office of ...
Basic Research Needs for Solar Energy Utilization - Office of ...
Basic Research Needs for Solar Energy Utilization - Office of ...
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LH1-RC<br />
35 ps<br />
HOW DO PHOTOSYNTHETIC ORGANISMS CAPTURE LIGHT AND SEPARATE CHARGE?<br />
<strong>Energy</strong> Flow within Bacterial Antenna Proteins<br />
and Funneling to the Reaction Center<br />
B850-B850<br />
100-200 fs<br />
LH2-LH1<br />
3-5 ps<br />
B800-B850<br />
1.2 ps<br />
B800-B800<br />
500 fs<br />
38<br />
The image to the left shows the detailed molecular<br />
structures <strong>of</strong> the two light-harvesting proteins, LH1<br />
and LH2, and the reaction center (RC) from a<br />
specific species <strong>of</strong> purple photosynthetic bacteria.<br />
The view is looking down onto the plane <strong>of</strong> the<br />
membrane in which these proteins reside. Green<br />
plant photosynthesis uses a larger number <strong>of</strong><br />
proteins, as well as greater numbers <strong>of</strong> energy and<br />
electron transfer c<strong>of</strong>actors. The bacterial system is<br />
illustrative because the issues and questions<br />
concerning how energy and electrons flow within and<br />
between proteins are similar <strong>for</strong> all photosynthetic<br />
organisms.<br />
The purpose <strong>of</strong> LH1 and LH2 is to increase the number <strong>of</strong> solar photons captured and to funnel them into the RC. The closely spaced<br />
bacteriochlorophyll molecules shown in green (above) transfer energy within LH1 and LH2 very rapidly, as indicated; this transfer is<br />
followed by somewhat slower transfer to the RC. Rapid energy transfer results in efficient utilization <strong>of</strong> the photon energy.<br />
Periplasm<br />
Membrane edge<br />
Car<br />
Membrane edge<br />
Cytoplasm<br />
Photoinduced Charge Separation in a<br />
Bacterial Reaction Center<br />
B Side<br />
BChl a<br />
BChl a 2<br />
(P865)<br />
+.<br />
0.9 ps<br />
BPh a BPh a<br />
Q B<br />
200 μs<br />
3.5 ps<br />
BChl a<br />
-. 200 ps<br />
Q A<br />
A Side<br />
The image to the left shows a side-on view <strong>of</strong> the RC<br />
in the photosynthetic membrane. Only the c<strong>of</strong>actors<br />
responsible <strong>for</strong> photo-induced charge separation<br />
across the membrane are shown. Excitation <strong>of</strong> the<br />
bacteriochlorophyll dimer (BChl a2) results in rapid<br />
electron transfer to an adjacent BChl a acceptor<br />
followed by thermal electron transfer to a<br />
bacteriopheophytin acceptor (a magnesium-free<br />
BChl a that is a better electron acceptor than BChl<br />
a). Two more thermal electron transfer events to<br />
quinone molecules, QA and QB, continue to move the<br />
electron further from the hole that remains on BChl<br />
a2. The result is separation <strong>of</strong> a single electron-hole<br />
pair across a 40-Å membrane with nearly 100%<br />
quantum efficiency.<br />
The high quantum efficiency <strong>of</strong> photosynthetic charge separation within the RC results principally from two important features <strong>of</strong> the<br />
structures <strong>of</strong> the protein and the electron donor-acceptor c<strong>of</strong>actors. First, the energetics <strong>for</strong> each electron transfer step are optimized to<br />
give the fastest <strong>for</strong>ward rate and the slowest back reaction rate. Second, the electron and hole are moved further away from one<br />
another with each electron transfer step, resulting in progressively weaker interactions between them. These factors combine to yield a<br />
very long-lived charge separation.