The adenylate kinase reaction acts as a frequency filter towards fluctuations of ATP utilization in the cell.
The buffering ability of the adenylate kinase reaction with respect to the phosphate potential and efficiency of oxidative phosphorylation in the presence of a fluctuating load conductance were studied by computer simulations. Fluctuations of the load conductance, i.e., of the irreversible ATP-utilizing reactions in the cell, were generated by integrating an Ornstein-Uhlenbeck diffusion process. This real or colored noise was then injected into the set of differential equations describing the rate laws for the changes of the adenine nucleotide concentrations based on a simple nonequilibrium thermodynamic model of oxidative phosphorylation. Numerical integration of this system of stochastic differential equations allowed us to investigate the influence of different parameters on the performance of this energy converter. Probability density estimates revealed that the variance of the efficiency about its optimal value was significantly reduced by the adenylate kinase reaction. It was found that the buffering ability of this enzyme is restricted to a specific frequency domain of the fluctuations of the load conductance. This frequency filtering was confirmed by substituting the random fluctuations of the load conductance by simple sinusoidal perturbations. All these studies revealed that for each domain of frequencies of the load perturbations there exists an optimal activity of the adenylate kinase which minimizes deviations from optimal efficiency of oxidative phosphorylation.
D000227:Adenine Nucleotides / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000263:Adenylate Kinase / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D010085:Oxidative Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D013816:Thermodynamics
D000227:Adenine Nucleotides; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D000263:Adenylate Kinase