التفاصيل البيبلوغرافية
| العنوان: |
FTIR spectroscopy shows weak symmetric hydrogen bonding of the Q Bcarbonyl groups in Rhodobacter sphaeroidesR26 reaction centres |
| المؤلفون: |
Brudler, R., de Groot, H.J.M., van Liemt, W.B.S., Gast, P., Hoff, A.J., Lugtenburg, J., Gerwert, K. |
| المصدر: |
FEBS Letters; January 1995, Vol. 370 Issue: 1 p88-92, 5p |
| مستخلص: |
The absorption frequencies of the C O and C C (neutral state) and of the CO (semiquinone state) stretching vibrations of Q Bhave been assigned by FTIR spectroscopy, using native and site-specifically 1-, 2-, 3- and 4- 13C-labelled ubiquinone-10 (UQ 10) reconstituted at the Q Bbinding site of Rhodobacter sphaeroidesR26 reaction centres. Besides the main C O band at 1641 cm −1, two smaller bands are observed at 1664 and 1651 cm −1. The smaller bands at 1664 and 1651 cm −1agree in frequencies with the 1- and 4-C O vibrations of unbound UQ 10, showing that a minor fraction is loosely and symmetrically bound to the protein. The larger band at 1641 cm −1indicates symmetric H-bonding of the 1- and 4-C O groups for the layer fraction of UQ 10but much weaker interaction as for the 4-C O group of Q AThe FTIR experiments show that different C O protein interactions contribute to the factors determining the different functions of UQ 10at the Q Aand the Q Bbinding sites. |
| قاعدة البيانات: |
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