Category:Complex:ATP synthase: Difference between revisions
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{{YouTube|uOoHKCMAUMc|Animation of ATP Synthase|250|right}} | {{YouTube|uOoHKCMAUMc|Animation of ATP Synthase|250|right}} | ||
ATP Synthase (aka F<sub>O</sub>F<sub>1</sub>-ATP synthase or F-type ATPase) is one of the central enzymes in energy metabolism for most organisms. It is a membrane protein found in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane of bacteria. Structurally ATP synthase is composed of two portions: hydrophobic membrane-embedded F<sub>O</sub> and hydrophilic F<sub>1</sub> that protrudes by approximately 10 nm from the membrane plane. | ATP Synthase (aka F<sub>O</sub>F<sub>1</sub>-ATP synthase or F-type ATPase) is one of the central enzymes in energy metabolism for most organisms. It is a membrane protein found in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane of bacteria. Structurally ATP synthase is composed of two portions: hydrophobic membrane-embedded F<sub>O</sub> and hydrophilic F<sub>1</sub> that protrudes by approximately 10 nm from the membrane plane. | ||
Both portions are multisubunit complexes. In <i>E. coli</i> F<sub>O</sub> is composed of subunits <i>a</i>, <i>b</i> and <i>c</i> in stoichiometry 1:2:10; F<sub>1</sub> consists of subunits alpha, beta, gamma, delta and epsilon in stoichiometry of 3:3:1:1:1. | Both portions are multisubunit complexes. In <i>E. coli</i> F<sub>O</sub> is composed of subunits <i>a</i>, <i>b</i> and <i>c</i> in stoichiometry 1:2:10; F<sub>1</sub> consists of subunits alpha, beta, gamma, delta and epsilon in stoichiometry of 3:3:1:1:1. | ||
In most organisms including E. coli ATP synthase uses energy stored in a proton electrochemical potential gradient to make ATP from ADP + P<sub>i</sub>. In some other bacteria, e.g. <i>Propionigenium modestum</i> or <i>Iliobacter tartaricus</i> sodium ion gradient energy is used. | In most organisms including <i>E. coli</i> ATP synthase uses energy stored in a proton electrochemical potential gradient to make ATP from ADP + P<sub>i</sub>. In some other bacteria, e.g. <i>Propionigenium modestum</i> or <i>Iliobacter tartaricus</i> sodium ion gradient energy is used. | ||
During ATP synthesis protons pass through F<sub>O</sub> and cause rotation of a ring-shape oligomer of 10 <i>c</i> subunits relative to the peripheral ab<sub>2</sub>-complex. This rotation is mechanically passed to subunits gamma and epsilon in F<sub>1</sub>. The rotation of | During ATP synthesis protons pass through F<sub>O</sub> and cause rotation of a ring-shape oligomer of 10 <i>c</i> subunits relative to the peripheral ab<sub>2</sub>-complex. This rotation is mechanically passed to subunits gamma and epsilon in F<sub>1</sub>. The rotation of gamma-epsilon complex relative to other F<sub>1</sub> subunits causes the co-ordinated binding and release of nucleotides and P<sub>i</sub> and results in ATP synthesis. | ||
"Proton translocation and ATP synthesis (or hydrolysis) are coupled by a unique mechanism, subunit rotation. Electrochemical energy contained in the proton gradient is converted into mechanical energy in form of subunit rotation, and back into chemical energy as ATP". <ref name='PMID:16730323'/> <br clear ='all'/> | "Proton translocation and ATP synthesis (or hydrolysis) are coupled by a unique mechanism, subunit rotation. Electrochemical energy contained in the proton gradient is converted into mechanical energy in form of subunit rotation, and back into chemical energy as ATP". <ref name='PMID:16730323'/> <br clear ='all'/> | ||
Revision as of 03:36, 11 September 2009
| uOoHKCMAUMc|250}} |
| Animation of ATP Synthase |
ATP Synthase (aka FOF1-ATP synthase or F-type ATPase) is one of the central enzymes in energy metabolism for most organisms. It is a membrane protein found in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane of bacteria. Structurally ATP synthase is composed of two portions: hydrophobic membrane-embedded FO and hydrophilic F1 that protrudes by approximately 10 nm from the membrane plane. Both portions are multisubunit complexes. In E. coli FO is composed of subunits a, b and c in stoichiometry 1:2:10; F1 consists of subunits alpha, beta, gamma, delta and epsilon in stoichiometry of 3:3:1:1:1.
In most organisms including E. coli ATP synthase uses energy stored in a proton electrochemical potential gradient to make ATP from ADP + Pi. In some other bacteria, e.g. Propionigenium modestum or Iliobacter tartaricus sodium ion gradient energy is used.
During ATP synthesis protons pass through FO and cause rotation of a ring-shape oligomer of 10 c subunits relative to the peripheral ab2-complex. This rotation is mechanically passed to subunits gamma and epsilon in F1. The rotation of gamma-epsilon complex relative to other F1 subunits causes the co-ordinated binding and release of nucleotides and Pi and results in ATP synthesis.
"Proton translocation and ATP synthesis (or hydrolysis) are coupled by a unique mechanism, subunit rotation. Electrochemical energy contained in the proton gradient is converted into mechanical energy in form of subunit rotation, and back into chemical energy as ATP". [1]
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