page_title: ATP synthase
section_title: Structure and function
hierarchical_section_title: ATP synthase / Structure and function
context_page_description: ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate, forming it from adenosine diphosphate and inorganic phosphate. The overall reaction catalyzed by ATP synthase is:
  ADP + Pᵢ + 3H⁺ₒᵤₜ ⇌ ATP + H₂O + 3H⁺ᵢₙ
  The formation of ATP from ADP and Pᵢ is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward, ATP synthase couples ATP synthesis during cellular respiration to an electrochemical gradient created by the difference in proton concentration across the mitochondrial plasma membrane in eukaryotes or the plasma membrane in bacteria. During photosynthesis in plants, ATP is synthesized by ATP synthase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma.
  ATP synthase is an F-ATPase. It consists of two main subunits, FO and F₁, which has a rotational motor mechanism allowing for ATP production. Because of its rotating subunit, ATP synthase is a molecular machine.
context_section_description: Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions  FO and F₁. FO causes rotation of  F₁ and is made of  c-ring and subunits a, two b, F6. F₁ is made of  α, β, γ, δ  subunits. F₁ has a water-soluble part that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO  F₁ creates a pathway for protons movement across the membrane.
caption: Simplified model of FOF1-ATPase alias ATP synthase of E. coli. Subunits of the enzyme are labeled accordingly.
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