ATP Synthase - Biochemistry

The electron transport chain moves high energy electrons through its complexes in order to create a proton gradient across the mitochondrial inner membrane. The ATP synthase then uses this gradient to pass hydrogen atoms through it. Because this is a favorable movement, it can be coupled to unfavorable processes such as conversion of ADP to ATP.

ATP synthase catalyzes the reaction that shows ADP and the phosphate group forming ATP. The hydrogen in the reactant side is the one involved in the proton gradient, and water is a byproduct of the reaction.

ATP synthase is located in the inner mitochondrial membrane. It has an F0 portion within the membrane and an F1 portion in the matrix. The F1 portion has a hexameric ring structure and is responsible for the creation of ATP from mechanical energy. The alpha, beta, and gamma subunits are all parts of the F1 portion of ATP synthase, however it is only the alpha and beta subunits that form the ring. Further, the beta subunit is the part of the ring that is considered to be catalytic.

ATP synthase can indeed produce more than 100 ATP molecules per second, and in the process, it only requires a few -- three or four -- protons, per ATP. These protons pass down a gradient through the membrane. Hence, the protein is membrane-bound. The protons cause the rotor of 10-14 subunits to spin. The protein's head itself has six subunits, three of which have ADP binding and phosphate binding sites.

The electron transport chain moves high energy electrons through its complexes in order to create a proton gradient across the mitochondrial inner membrane. The ATP synthase then uses this gradient to pass hydrogen atoms through it. Because this is a favorable movement, it can be coupled to unfavorable processes such as conversion of ADP to ATP.

ATP synthase catalyzes the reaction that shows ADP and the phosphate group forming ATP. The hydrogen in the reactant side is the one involved in the proton gradient, and water is a byproduct of the reaction.

ATP synthase is located in the inner mitochondrial membrane. It has an F0 portion within the membrane and an F1 portion in the matrix. The F1 portion has a hexameric ring structure and is responsible for the creation of ATP from mechanical energy. The alpha, beta, and gamma subunits are all parts of the F1 portion of ATP synthase, however it is only the alpha and beta subunits that form the ring. Further, the beta subunit is the part of the ring that is considered to be catalytic.

ATP synthase can indeed produce more than 100 ATP molecules per second, and in the process, it only requires a few -- three or four -- protons, per ATP. These protons pass down a gradient through the membrane. Hence, the protein is membrane-bound. The protons cause the rotor of 10-14 subunits to spin. The protein's head itself has six subunits, three of which have ADP binding and phosphate binding sites.

The electron transport chain moves high energy electrons through its complexes in order to create a proton gradient across the mitochondrial inner membrane. The ATP synthase then uses this gradient to pass hydrogen atoms through it. Because this is a favorable movement, it can be coupled to unfavorable processes such as conversion of ADP to ATP.

ATP synthase catalyzes the reaction that shows ADP and the phosphate group forming ATP. The hydrogen in the reactant side is the one involved in the proton gradient, and water is a byproduct of the reaction.

ATP synthase is located in the inner mitochondrial membrane. It has an F0 portion within the membrane and an F1 portion in the matrix. The F1 portion has a hexameric ring structure and is responsible for the creation of ATP from mechanical energy. The alpha, beta, and gamma subunits are all parts of the F1 portion of ATP synthase, however it is only the alpha and beta subunits that form the ring. Further, the beta subunit is the part of the ring that is considered to be catalytic.

ATP synthase can indeed produce more than 100 ATP molecules per second, and in the process, it only requires a few -- three or four -- protons, per ATP. These protons pass down a gradient through the membrane. Hence, the protein is membrane-bound. The protons cause the rotor of 10-14 subunits to spin. The protein's head itself has six subunits, three of which have ADP binding and phosphate binding sites.

The electron transport chain moves high energy electrons through its complexes in order to create a proton gradient across the mitochondrial inner membrane. The ATP synthase then uses this gradient to pass hydrogen atoms through it. Because this is a favorable movement, it can be coupled to unfavorable processes such as conversion of ADP to ATP.

ATP synthase catalyzes the reaction that shows ADP and the phosphate group forming ATP. The hydrogen in the reactant side is the one involved in the proton gradient, and water is a byproduct of the reaction.

ATP synthase is located in the inner mitochondrial membrane. It has an F0 portion within the membrane and an F1 portion in the matrix. The F1 portion has a hexameric ring structure and is responsible for the creation of ATP from mechanical energy. The alpha, beta, and gamma subunits are all parts of the F1 portion of ATP synthase, however it is only the alpha and beta subunits that form the ring. Further, the beta subunit is the part of the ring that is considered to be catalytic.