ATP Synthase Definition
ATP synthase is an enzyme that catalyzes the formation of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate (Pi). It is located in the mitochondrial inner membrane and uses a form of energy, such as the proton gradient, to drive the synthesis.
The function of ATP Synthase
ATP synthase is an enzyme that catalyzes the formation of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP is the main energy molecule used in cells, and ATP synthase produces it during cellular respiration. The enzyme is found in all life forms and powers all cellular activities.
The function of ATP synthase is to produce ATP by using energy derived from a gradient of protons that cross the inner mitochondrial membrane from the intermembrane space into the matrix through the Fo portion of the enzyme.
Each ATP synthase can produce about 100 molecules of ATP every second. In eukaryotic cells, ATP synthase lies across the inner mitochondrial membrane, while in prokaryotic cells, it lies across the plasma membrane.
Organisms capable of photosynthesis also have ATP synthase across the thylakoid membrane, which in plants is located in chloroplasts.
The structure of ATP synthase consists of two parts, F0 and F1. The F0 part spans the membrane and conducts protons into or out of mitochondria or bacteria.
The F1 part protrudes into the mitochondrial matrix or bacterial cytoplasm where it synthesizes ATP from ADP and Pi using energy derived from proton flow through F0.
Structure of ATP Synthase
ATP synthase is a molecular machine that catalyzes the formation of adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi).
It consists of two well-defined protein entities: the F1 sector, a soluble portion situated in the mitochondrial matrix, and the Fo sector, bound to the inner mitochondrial membrane.
The F1 sector is composed of three copies of each of subunits α and β, and one each of subunits γ, δ, and ε. The Fo sector causes the rotation of F1 and is made up of several subunits.
The cryo-EM structure of a divergent ATP synthase dimer from the mitochondria of Euglena gracilis has been reported. It features 29 different subunits, 8 of which are unique compared to all previously characterized ATP synthases. The newly found elements are involved in proton transfer.
ATP synthase is a complex structure consisting of two domains Fo and F1. F1 is a spherical structure that sticks out into the mitochondrial matrix while Fo spans the inner membrane.
ATP synthesis is the process of producing ATP (adenosine triphosphate) molecules from ADP (adenosine diphosphate) and phosphate. It is primarily carried out in the cellular respiration process, where respiratory substrates such as carbohydrates, lipids, and proteins are oxidized to produce energy which is stored in the form of high-energy bonds in ATP.
Most ATP formation takes place in the electron transport chain by oxidative phosphorylation. The enzyme ATP synthase catalyzes the synthesis of ATP. In mitochondria, a proton gradient is created across the inner membrane which drives protons through the membrane and powers ATP synthesis.
The F 1 subunit of ATP synthase contains a membrane-spanning domain and a knobby protrusion that extends into the matrix, which catalyzes the formation of phosphodiester bonds between ADP and phosphate to form ATP.
During photosynthesis, solar energy splits two molecules of H2O into molecular oxygen and hydrogen ions which are used to generate a proton gradient for ATP synthesis.