Lipids affect the charge stabilization in wild-type and mutant reaction centers of Rhodobacter sphaeroides R-26

1999 ◽  
Vol 26 (5) ◽  
pp. 465 ◽  
Author(s):  
László Nagy ◽  
Elfrida Fodor ◽  
Júlia Tandori ◽  
László Rinyu ◽  
Tibor Farkas

The effect of lipids on stabilization of electrons on the secondary quinone was studied in reaction centers (RC) of herbicide-sensitive and -resistant (L229Ile → Met) Rhodobacter sphaeroides R-26. The lipid concentration and the lipid/protein ratio of the intracytoplasmic membranes (ICM) were larger in the mutant RCs than in the wild-type. The free energy changes of Q A – Q B → Q A Q B – electron transfer were ΔG 0 = –57 meV, –69 meV, –85 meV for the wild-type and ΔG 0 = 0 meV, –15 meV, –46 meV for the mutant at pH = 8.0, in detergent, liposome and ICM, respectively. The differences in the stabilization energies of both strains decreased from the detergent via proteoliposome to chromatophore. We conclude that the energetics of the interquinone electron transfer depends on the environment of the reaction center. The steric and/or electrostatic interactions of the environment and Q B pocket can modulate the energetics of the charge stabilization over large distances. The interaction may have crucial importance on coupling the electron transport in the photosynthetic membrane to the anabolic/catabolic processes taking place in the cells.

2015 ◽  
Vol 112 (11) ◽  
pp. 3397-3402 ◽  
Author(s):  
Christoph von Ballmoos ◽  
Nathalie Gonska ◽  
Peter Lachmann ◽  
Robert B. Gennis ◽  
Pia Ädelroth ◽  
...  

The ba3-type cytochrome c oxidase from Thermus thermophilus is a membrane-bound protein complex that couples electron transfer to O2 to proton translocation across the membrane. To elucidate the mechanism of the redox-driven proton pumping, we investigated the kinetics of electron and proton transfer in a structural variant of the ba3 oxidase where a putative “pump site” was modified by replacement of Asp372 by Ile. In this structural variant, proton pumping was uncoupled from internal electron transfer and O2 reduction. The results from our studies show that proton uptake to the pump site (time constant ∼65 μs in the wild-type cytochrome c oxidase) was impaired in the Asp372Ile variant. Furthermore, a reaction step that in the wild-type cytochrome c oxidase is linked to simultaneous proton uptake and release with a time constant of ∼1.2 ms was slowed to ∼8.4 ms, and in Asp372Ile was only associated with proton uptake to the catalytic site. These data identify reaction steps that are associated with protonation and deprotonation of the pump site, and point to the area around Asp372 as the location of this site in the ba3 cytochrome c oxidase.


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