Abstract
Photo-excitation of membrane-bound Rhodobacter sphaeroides reaction centres containing the mutation Ala M260 to Trp (AM260W) resulted in the accumulation of a radical pair state involving the photo-oxidised primary electron donor (P). This state had a lifetime of hundreds of milliseconds and its formation was inhibited by stigmatellin. The absence of the QA ubiquinone in the AM260W reaction centre suggests that this long-lived radical pair state is P+QB-, although the exact reduction/protonation state of the QB quinone remains to be confirmed. The blockage of active branch (A-branch) electron transfer by the AM260W mutation implies that this P+QB- state is formed by electron transfer along the so-called inactive branch (B-branch) of reaction centre cofactors. We discuss how further mutations may affect the yield of the P+QB- state, including a double alanine mutation (EL212A/DL213A) that probably has a direct effect on the efficiency of the low yield electron transfer step from the anion of the B-branch bacteriopheophytin (HB-) to the QB ubiquinone. © 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 234-240 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 540 |
| Issue number | 1-3 |
| DOIs | |
| Publication status | Published - 10 Apr 2003 |
Keywords
- Electron transfer
- Inactive branch
- Mutagenesis
- Photosynthesis
- Reaction centre
- Spectroscopy
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