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Identification of a hydrogen bond in the Phe M197→Tyr mutant reaction center of the photosynthetic purple bacterium Rhodobacter sphaeroides by X-ray crystallography and FTIR spectroscopy

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Kuglstatter,  Andreas
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Fritzsch,  Günter
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Wachtveitl,  Josef
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Oesterhelt,  Dieter
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kuglstatter, A., Hellwig, P., Fritzsch, G., Wachtveitl, J., Oesterhelt, D., Mäntele, W., et al. (1999). Identification of a hydrogen bond in the Phe M197→Tyr mutant reaction center of the photosynthetic purple bacterium Rhodobacter sphaeroides by X-ray crystallography and FTIR spectroscopy. FEBS Letters, 463(1-2), 169-174. doi:10.1016/s0014-5793(99)01614-2.


Cite as: https://hdl.handle.net/21.11116/0000-0007-5958-3
Abstract
In bacterial reaction centers the charge separation process across the photosynthetic membrane is predominantly driven by the excited state of the bacteriochlorophyll dimer (D). An X-ray structure analysis of the Phe M197→Tyr mutant reaction center from Rhodobacter sphaeroides at 2.7 Å resolution suggests the formation of a hydrogen bond as postulated by Wachtveitl et al. [Biochemistry 32, 12875–12886, 1993] between the Tyr M197 hydroxy group and one of the 2a-acetyl carbonyls of D. In combination with electrochemically induced FTIR difference spectra showing a split band of the π-conjugated 9-keto carbonyl of D, there is clear evidence for the existence of such a hydrogen bond.