Modeling the Q-cycle mechanism of transmembrane energy conversion.
The Q-cycle mechanism plays an important role in the conversion of the redox energy into the energy of the proton electrochemical gradient across the biomembrane. The bifurcated electron transfer reaction, which is built into this mechanism, recycles one electron, thus allowing us to translocate two protons per one electron moving to the high-potential redox chain. We study a kinetic model of the Q-cycle mechanism in an artificial system which mimics the bf complex of plants and cyanobacteria in the regime of ferredoxin-dependent cyclic electron flow. Using methods of condensed matter physics, we derive a set of master equations and describe a time sequence of electron and proton transfer reactions in the complex. We find energetic conditions when the bifurcation of the electron pathways at the positive side of the membrane occurs naturally, without any additional gates. For reasonable parameter values, we show that this system is able to translocate more than 1.8 protons, on average, per one electron, with a thermodynamic efficiency of the order of 32% or higher.
Advanced Science Institute, RIKEN, Wako-shi, Saitama 351-0198, Japan. asmirnov@riken.jp
Anatoly Yu
AY
Smirnov
Franco
F
Nori
D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D000458:Cyanobacteria / Q000166:cytology / Q000378:metabolism; D045346:Cytochrome b6f Complex / Q000378:metabolism*; D004058:Diffusion; D004579:Electron Transport; D004583:Electrons; D005288:Ferredoxins / Q000378:metabolism; D007700:Kinetics; D008954:Models, Biological; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D018892:Proton-Motive Force; D011522:Protons; D013816:Thermodynamics
D001426:Bacterial Proteins; D005288:Ferredoxins; D010940:Plant Proteins; D011522:Protons; D045346:Cytochrome b6f Complex