The outgoing voltage delivered to the outer circuit is then given by Ue = −Δϕ = +8 V. Lc1 and Lc2 are given by –5/2 and 5/3 Ω−1, respectively, or Ri1 = −0.4, and Ri2 = 0.6 Ω, which fulfils Ri1 + Ri2 = Ri = 0.2 Ω. Setting Re = 4.0 Ω yields Ri1 = −4.0, Ri2 = 4.2 Ω, and again Ri = 0.2 Ω. Moreover, in the electric circuit the overall resistance Ri1 + Re vanishes. It should be noticed that partial resistances are not constant, although

Ri is a constant. They depend both on Re and Le, respectively. The total dissipation function of reactions in the battery and of the outer circuit is given by: Фcirc = Ф1 + Ф2 + Фe = I(Δϕ Inhibitors,research,lifescience,medical + E + U), Фcirc = I × E(240 J/s or 0.24 kW), or (A3a) Фcirc = Lc2 × E2 (1/0.6×144 = 0.24 kW) (A3b) This latter result means that the total entropy production of the circuit is given by that of the redox reaction. This is also valid with respect to heat production. Power output as a function of Re is

given by: (A4a) , or Maximal power output is reached at Re = Ri = 0.2 Ω, poutmax = 0.18 kW. Because Pout can also be expressed Inhibitors,research,lifescience,medical as Pout = -Lc1 × Δϕ2, this yields with Le = 1/0.2 1/Ω, poutmax = −(−5.0)( −6)2 = 0.18 kW. When a second battery is added to the circuit in such a way that EII is directed against EI (EII = −10.9 V, RiII = 0.5 Ω), ΔϕII is now positive and EII negative. The outer resistance Re stands for the resistance of the wires connecting both batteries. In this constellation, Inhibitors,research,lifescience,medical −ΔϕI is no longer equal to Ue. Now − (ΔϕI+ Ue) = −ΔϕIe = ΔϕII is valid. Consequently, Re also has to be added to RiI yielding RiIe = RiI+ Re. (A4b) from: , and (A4c) Δ ϕIe = −11.4 V, and ΔϕII = 11.4 V is obtained. Partial Inhibitors,research,lifescience,medical conductances are given by: (A4d) Again, the overall resistance of the electric path in the circuit is zero. The total resistance RiI + Re + RiII = Inhibitors,research,lifescience,medical 1.1 Ω, therefore, is also given by Ri2I + Ri1II = 12 + (–10.9) = 1.1 Ω. ATP, ADP, and Pi Species as Functions of [H+] and [Mg2+] ATP species, including MgATP2−, are calculated according to the methods of Alberty [20]. When respective constants

are known, which are dependent on temperature and ionic because strength, so-called polynomials can be formulated, from which several parameters like species concentration, K’(biochemical equilibrium constant), Carfilzomib or [H+] and [Mg2+] binding can be taken. ATP splitting by myosin ATPase is formulated here for the species MgATP2−, MgADP−, and H2PO4−, to make the reactions of the cross-bridge cycle directly dependent on these compounds. The reaction in chemical notation form is given by: The equilibrium Nintedanib clinical constant for the above reaction is given by: (A5a) (A5b) (A5c) Kref1 (= 6.267 × 105), K3at, K3ad, PATP4−, and PADP3− were taken from [1]. At given [H+] and [Mg2+] values, the corresponding K’(= 4.9687 × 105, pH = 7.1, [Mg2+] = 800 µM) is identical to formulations with other reference constants. [H+] and [Mg2+] Buffering [H+] buffering of SMFs is treated here analogously to VMs (see [1]).