Dehydration affects the electronic structure of the primary electron donor in bacterial photosynthetic reaction centers: evidence from visible-NIR and light-induced difference FTIR spectroscopy

Photochem Photobiol Sci. 2015 Feb;14(2):238-51. doi: 10.1039/c4pp00245h.

Abstract

The photosynthetic reaction center (RC) is a membrane pigment-protein complex that catalyzes the initial charge separation reactions of photosynthesis. Following photoexcitation, the RC undergoes conformational relaxations which stabilize the charge-separated state. Dehydration of the complex inhibits its conformational dynamics, providing a useful tool to gain insights into the relaxational processes. We analyzed the effects of dehydration on the electronic structure of the primary electron donor P, as probed by visible-NIR and light-induced FTIR difference spectroscopy, in RC films equilibrated at different relative humidities r. Previous FTIR and ENDOR spectroscopic studies revealed that P, an excitonically coupled dimer of bacteriochlorophylls, can be switched between two conformations, P866 and P850, which differ in the extent of delocalization of the unpaired electron between the two bacteriochlorophyll moieties (PL and PM) of the photo-oxidized radical P(+). We found that dehydration (at r = 11%) shifts the optical Qy band of P from 866 to 850-845 nm, a large part of the effect occurring already at r = 76%. Such a dehydration weakens light-induced difference FTIR marker bands, which probe the delocalization of charge distribution within the P(+) dimer (the electronic band of P(+) at 2700 cm(-1), and the associated phase-phonon vibrational modes at around 1300, 1480, and 1550 cm(-1)). From the analysis of the P(+) keto C[double bond, length as m-dash]O bands at 1703 and 1713-15 cm(-1), we inferred that dehydration induces a stronger localization of the unpaired electron on PL(+). The observed charge redistribution is discussed in relation to the dielectric relaxation of the photoexcited RC on a long (10(2) s) time scale.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Electrons
  • Humidity
  • Phonons
  • Photochemical Processes
  • Photosynthetic Reaction Center Complex Proteins / chemistry*
  • Protein Conformation
  • Rhodobacter sphaeroides
  • Spectroscopy, Fourier Transform Infrared
  • Spectroscopy, Near-Infrared
  • Vibration
  • Water / chemistry*

Substances

  • Bacterial Proteins
  • Photosynthetic Reaction Center Complex Proteins
  • Water