Hydrogen bonds in the vicinity of the special pair of the bacterial reaction center probed by hydrostatic high-pressure absorption spectroscopy

Liina Kangur, Michael R. Jones, Arvi Freiberg*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

6 Citations (Scopus)
217 Downloads (Pure)

Abstract

Using the native bacteriochlorophyll a pigment cofactors as local probes, we investigated the response to external hydrostatic high pressure of reaction center membrane protein complexes from the photosynthetic bacterium Rhodobacter sphaeroides. Wild-type and engineered complexes were used with varied number (0, 1 or 2) of hydrogen bonds that bind the reaction center primary donor bacteriochlorophyll cofactors to the surrounding protein scaffold. A pressure-induced breakage of hydrogen bonds was established for both detergent-purified and membrane-embedded reaction centers, but at rather different pressures: between 0.2 and 0.3 GPa and at about 0.55 GPa, respectively. The free energy change associated with the rupture of the single hydrogen bond present in wild-type reaction centers was estimated to be equal to 13–14 kJ/mol. In the mutant with two symmetrical hydrogen bonds (FM197H) a single cooperative rupture of the two bonds was observed corresponding to about twice stronger bond, rather than a sequential rupture of two individual bonds.
Original languageEnglish
Pages (from-to)27-33
Number of pages7
JournalBiophysical Chemistry
Volume231
Early online date7 Apr 2017
DOIs
Publication statusPublished - 1 Dec 2017

Keywords

  • Membrane protein stability
  • H-bond energy
  • Hydrostatic high pressure
  • Cooperativity
  • Reaction center mutants
  • Photosynthesis
  • Rhodobacter sphaeroides

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