We study a system of qubits that are coupled to each other via only one degree of freedom represented, e.g., by $sigma_z$-operators. We prove that, if by changing the Hamiltonian parameters, a non-degenerate ground state of the system is continuously
transformed in such a way that the expectation values of $sigma_z$ operators of at least two coupled qubits change, this ground state is entangled. Using this proof, we discuss connection between energy level anticrossings and ground state entanglement. Following the same line of thought, we introduce entanglement witnesses, based on cross-susceptibilities, that can detect ground state entanglement for any bipartition of the multi-qubit system. A witness for global ground state entanglement is also introduced.
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 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.
We present two models for electron-driven uphill proton transport across lipid membranes, with the electron energy converted to the proton gradient via the electrostatic interaction. In the first model, associated with the cytochrome c oxidase comple
x in the inner mitochondria membranes, the electrostatic coupling to the site occupied by an electron lowers the energy level of the proton-binding site, making the proton transfer possible. In the second model, roughly describing the redox loop in a nitrate respiration of E. coli bacteria, an electron displaces a proton from the negative side of the membrane to a shuttle, which subsequently diffuses across the membrane and unloads the proton to its positive side. We show that both models can be described by the same approach, which can be significantly simplified if the system is separated into several clusters, with strong Coulomb interaction inside each cluster and weak transfer couplings between them. We derive and solve the equations of motion for the electron and proton creation/annihilation operators, taking into account the appropriate Coulomb terms, tunnel couplings, and the interaction with the environment. For the second model, these equations of motion are solved jointly with a Langevin-type equation for the shuttle position. We obtain expressions for the electron and proton currents and determine their dependence on the electron and proton voltage build-ups, on-site charging energies, reorganization energies, temperature, and other system parameters. We show that the quantum yield in our models can be up to 100% and the power-conversion efficiency can reach 35%.
We propose a simple model of cytochrome c oxidase, including four redox centers and four protonable sites, to study the time evolution of electrostatically coupled electron and proton transfers initiated by the injection of a single electron into the
enzyme. We derive a system of master equations for electron and proton state probabilities and show that an efficient pumping of protons across the membrane can be obtained for a reasonable set of parameters. All four experimentally observed kinetic phases appear naturally from our model. We also calculate the dependence of the pumping efficiency on the transmembrane voltage at different temperatures and discuss a possible mechanism of the redox-driven proton translocation.
Respiration in bacteria involves a sequence of energetically-coupled electron and proton transfers creating an electrochemical gradient of protons (a proton-motive force) across the inner bacterial membrane. With a simple kinetic model we analyze a r
edox loop mechanism of proton-motive force generation mediated by a molecular shuttle diffusing inside the membrane. This model, which includes six electron-binding and two proton-binding sites, reflects the main features of nitrate respiration in E. coli bacteria. We describe the time evolution of the proton translocation process. We find that the electron-proton electrostatic coupling on the shuttle plays a significant role in the process of energy conversion between electron and proton components. We determine the conditions where the redox loop mechanism is able to translocate protons against the transmembrane voltage gradient above 200 mV with a thermodynamic efficiency of about 37%, in the physiologically important range of temperatures from 250 to 350 K.
Shuttle-assisted charge transfer is pivotal for the efficient energy transduction from the food-stuff electrons to protons in the respiratory chain of animal cells and bacteria. The respiratory chain consists of four metalloprotein Complexes (I-IV) e
mbedded in the inner membrane of a mitochondrion. Three of these complexes pump protons across the membrane, fuelled by the energy of food-stuff electrons. Despite extensive biochemical and biophysical studies, the physical mechanism of this proton pumping is still not well understood. Here we present a nanoelectromechanical model of the electron-driven proton pump related to the second loop of the respiratory chain, where a lipid-soluble ubiquinone molecule shuttles between the Complex I and Complex III, carrying two electrons and two protons. We show that the energy of electrons can be converted to the transmembrane proton potential gradient via the electrostatic interaction between electrons and protons on the shuttle. We find that the system can operate either as a proton pump, or, in the reverse regime, as an electron pump. For membranes with various viscosities, we demonstrate that the uphill proton current peaks near the body temperature $T approx 37 ^{circ}$C.
We analyze the dynamics of rotary biomotors within a simple nano-electromechanical model, consisting of a stator part and a ring-shaped rotor having twelve proton-binding sites. This model is closely related to the membrane-embedded F$_0$ motor of ad
enosine triphosphate (ATP) synthase, which converts the energy of the transmembrane electrochemical gradient of protons into mechanical motion of the rotor. It is shown that the Coulomb coupling between the negative charge of the empty rotor site and the positive stator charge, located near the periplasmic proton-conducting channel (proton source), plays a dominant role in the torque-generating process. When approaching the source outlet, the rotor site has a proton energy level higher than the energy level of the site, located near the cytoplasmic channel (proton drain). In the first stage of this torque-generating process, the energy of the electrochemical potential is converted into potential energy of the proton-binding sites on the rotor. Afterwards, the tangential component of the Coulomb force produces a mechanical torque. We demonstrate that, at low temperatures, the loaded motor works in the shuttling regime where the energy of the electrochemical potential is consumed without producing any unidirectional rotation. The motor switches to the torque-generating regime at high temperatures, when the Brownian ratchet mechanism turns on. In the presence of a significant external torque, created by ATP hydrolysis, the system operates as a proton pump, which translocates protons against the transmembrane potential gradient. Here we focus on the F$_0$ motor, even though our analysis is applicable to the bacterial flagellar motor.
We examine the dynamics of biological nanomotors within a simple model of a rotor having three ion-binding sites. It is shown that in the presence of an external dc electric field in the plane of the rotor, the loading of the ion from the positive si
de of a membrane (rotor charging) provides a torque leading to the motor rotation. We derive equations for the proton populations of the sites and solve these equations numerically jointly with the Langevin-type equation for the rotor angle. Using parameters for biological systems, we demonstrate that the sequential loading and unloading of the sites lead to the unidirectional rotation of the motor. The previously unexplained phenomenon of fast direction-switching in the rotation of a bacterial flagellar motor can also be understood within our model.
We examine a simple model of proton pumping through the inner membrane of mitochondria in the living cell. We demonstrate that the pumping process can be described using approaches of condensed matter physics. In the framework of this model, we show
that the resonant Forster-type energy exchange due to electron-proton Coulomb interaction can provide an unidirectional flow of protons against an electrochemical proton gradient, thereby accomplishing proton pumping. The dependence of this effect on temperature as well as electron and proton voltage build-ups are obtained taking into account electrostatic forces and noise in the environment. We find that the proton pump works with maximum efficiency in the range of temperatures and transmembrane electrochemical potentials which correspond to the parameters of living cells.
