Question: A 250-V, 4-pole, wave-wound d.c. series motor has 782 conductors on itsarmature. It has armature and series field resistance of 0.75 ohm. The motor takesa current of 40 A. Estimate its speed and gross torque developed if it has a flux per pole of 25 mWb Answer: Step 1 Mechanical Engineering homework question answer, step 1, image 1 Mechanical Engineering homework question answer, step 1, image 2 Step 2 Mechanical Engineering homework question answer, step 2, image 1 Step 3 Mechanical Engineering homework question answer, step 3, image 1

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Answer:

1. If the metabolic conditions dictate the form of ATP synthase that varies, such that a single membrane contains ATP synthases with different c ring structures, then there is a chance that the overall energetics would be dictated by those molecules with the smallest c rings and proton per ATP stoichiometries. Similarly, it is not easy for the size of the c ring to vary in a membrane in response to different metabolic fluxes. The c ring is tightly linked to the γ and ϵ subunits. Thus, as the c ring turns, these subunits are turned inside the α3β3 hexamer unit of F1. The rotation of the proton-gradient is driven by the c ring that drives the rotation of the γ subunit,  which in turn promotes the synthesis of ATP through the binding-change mechanism. The number of c subunits in the c ring appears to range between 10 and 14. This number is significant because it determines the number of protons that must be transported to generate a molecule of ATP. Each 360-degree rotation of the γ subunit leads to the synthesis and release of three molecules of ATP. Thus, if there are 10 c subunits in the ring (as was observed in a crystal structure of yeast mitochondrial ATP synthase), each ATP generated requires the transport of 10/3 = 3.33 protons.

2.  The core subunits of both F0 and F1 portions are highly conserved, with the striking exception that the number of c subunits that compose the F0 ring varies from 8 to 17. ATP synthesis in F0F1 ATP synthase involves rotational catalysis movement of the membrane embedded F0 portion driven by a single ion binding by each c–subunit, which is coupled to the catalytic turnover of the F1 α3β3 hexamer to release three ATP molecules per full turnover of the complex.  In this mechanism, a full turnover of the F1 enzyme is coupled to complete 360° rotation of the c–ring, generating three ATP per c-subunits, dictating that the number of protons required to generate three ATPs (n H+/ATP) will be equal to the number of c-subunits. Overall energetics might change for an organism which is not feasible.