Biochemistry (Moscow)

, Volume 84, Issue 9, pp 1107–1115 | Cite as

Spectral and Photochemical Properties of Rhodobacter sphaeroides R-26 Reaction Center Films in Vacuum

  • A. A. ZabelinEmail author
  • V. A. Shkuropatova
  • V. A. Shuvalov
  • A. Ya. Shkuropatov


Using absorption spectroscopy in the visible/near-IR and mid-IR regions, spectral and photochemical properties of isolated reaction centers (RCs) from Rhodobacter sphaeroides R-26 were studied in dried films on the inorganic support surface (quartz or CaF2 plates) under vacuum dehydration conditions (10−2 or 7·10−5 mm Hg). Three detergents, N,N-dimethyldodecylamine N-oxide (LDAO), Triton X-100 (TX100), and n-dodecyl-β-D-maltoside (DM), were tested for their ability to stabilize the RC–detergent complexes in the vacuum-dried state. It was shown that in the presence of LDAO, RC complexes underwent destruction in vacuum. In contrast, DM provided an environment that minimized irreversible disruptive changes in the RCs in vacuum. The effects of vacuum dehydration on the RC–DM films included a small increase in the content of α-helices in the RC protein, a short-wavelength reversible shift in the optical transitions of pigments, and minor changes in the electronic structure of the P+ dimer. The films retained their photochemical activity upon excitation with high-intensity light (200 mW/cm2). TX100 also helped to maintain spectral and functional properties of the RCs in vacuum; however, in this case, the stabilizing effect was less pronounced than in the presence of DM, especially, at high detergent concentrations. The results are discussed within the framework of a model suggesting that the detergent-protein interactions and the properties of detergent micelles play a dominant role in maintaining the structure of the RCs upon vacuum dehydration of the RC complexes. The obtained data can be useful for developing hybrid photoconverting systems based on bacterial RCs.


reaction center absorption spectroscopy vacuum dehydration detergent micelles Rhodobacter sphaeroides R-26 



absorbance change



BA and BB

monomeric BChl molecules in branches A and B, respectively





FTIR spectroscopy

Fourier-transform infrared spectroscopy

HA and HB

BPheo molecules in branches A and B, respectively




primary electron donor, a dimer of BChl molecules

PA and PB

BChl molecules that form P


primary quinone acceptor


secondary quinone acceptor


reaction center


Triton X-100


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Funding. The study was conducted under the Government Contract no. AAAA-A17030110140-5 and partially supported by the Russian Foundation for Basic Research (project 16-34-00829).

Compliance with ethical standards. This study does not contain description of any research with animals or human participants performed by any of the authors.


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Copyright information

© Pleiades Publishing, Ltd. 2019

Authors and Affiliations

  • A. A. Zabelin
    • 1
    Email author
  • V. A. Shkuropatova
    • 1
  • V. A. Shuvalov
    • 1
  • A. Ya. Shkuropatov
    • 1
  1. 1.Institute of Basic Biological Problems, Pushchino Scientific Center for Biological ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia

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