![]() ![]() A portion of the F O (the ring of C-subunits) rotates as the protons pass through the membrane. Additional adenine nucleotide binding sites in α -subunits are regulatory.Īccording to the current model of ATP synthesis (known as the alternating catalytic model), the proton-motive force across the inner mitochondrial membrane, generated by the electron transport chain, drives the passage of protons through the membrane via the F O region of ATP synthase. Three substrate binding sites are in the β-subunits (Fig. A soluble portion, the F 1 ATP-ase, contains 5 subunits, in a stoichiometry of 3α:3β:1γ:1δ:1ε. The antibiotic oligomycin inhibits the F O unit of ATP synthase. The F 1 fraction derives its name from the term “Fraction 1” and F O (written as a subscript “O”, not “zero”) derives its name from being the oligomycin binding fraction. In F 1F O ATP synthase, the F O portion is within the membrane and the F 1 portion is above the membrane. F O is a cylindrical structure capable of rotation when driven by translocated protons and is linked to a central stalk that can revolve inside F 1. F 1 is a spherical structure, sticks out into the matrix and is anchored to the membrane, consists of three α- and three β- subunits, all of which can bind nucleotides, but only the β-subunits can take part in the reactions (Fig. ATP synthase is a complex structure consisting of two domains F O and F 1. This is all-important reactions in which the proton-motive force, produced by proton translocation, is coupled to the synthesis of ATP from ADP and phosphate. ![]() After reading this article you will learn about the structure and mechanism of ATP synthase, with the help of suitable diagrams.īoyer and Walker received the Nobel Prize in 1997 for elucidating the mechanism of ATP synthase. ![]()
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