Organisation of mitochondrial membranes and the electron transport chain. (a) False‐coloured transmission electron micrograph of a mitochondrion from and corresponding schematic diagram showing the organisation of mitochondrial membranes and division of the mitochondrion into six distinct compartments. (b) The mitochondrial ETC of a typical plant. The five complexes (complexes I–IV and ATP synthase) common to the standard ETC are shown in gold. Plant‐specific complexes (AOX and NAD(P)H oxidoreductases) are shown in green, whereas mobile electron carriers, ubiquinone and cytochrome , are shown in red. An uncoupling ND, NAD(P)H oxidoreductase; UQ, ubiquinone; AOX, alternate terminal oxidase; Cyt C, cytochrome ; PUMP, plant uncoupling mitochondrial protein. Protons are pumped from the matrix into the intermembrane and intercristal spaces. Bar, 0.1 μm. Electron micrograph, X–D Wang; drawings, MB Sheahan.
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Each chloroplast comprises a network of membranes that contain pigments and enzymes essential for harvesting light energy, and converting it into chemical energy.
Abu‐Abied M, Avisar D, Belausov E et al. (2009) Identification of an Arabidopsis unknown small membrane protein targeted to mitochondria, chloroplasts and peroxisomes. Protoplasma 236: 3–12.
A series of metabolic pathways (the Krebs cycle and others) in the mitochondria result in thefurther breaking of chemical bonds and the liberation of ATP.
In addition to ATP synthesis, prokaryotic cells can use the proton motive force to supply energy for active transport of molecules across the plasma membrane, and to power the motor complex that rotates the bacterial .
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We have seen how ATP synthase acts like a proton-powered turbine, and uses the energy released from the down-gradient flow of protons to synthesize ATP. The process of pumping protons across the membrane to generate the proton gradient is called . Chemiosmosis is driven by the flow of electrons down the electron transport chain, a series of protein complexes in the membrane that forms an electron bucket brigade. Each of these protein complexes accepts and passes on electrons down the chain, and pumps a proton across the membrane for each electron it passes on. Ultimately, the last complex in the electron transport chain passes the electrons to molecular oxygen (O2) to make water, in the case of aerobic respiration.
The ATP synthases in mitochondria, chloroplasts, and Bacteria are all structurally similar, and their amino acid sequence similarities are consistent with a common evolutionary origin (Watt et al. 2010). Lesser degrees of similarity, and more distant evolutionary relationships, exist with Archaeal ATP synthases and with vacuolar membrane ATPases. Vacuolar ATPases pump protons across the membrane using the energy from ATP hydrolysis. Indeed, Bacterial and mitochondrial ATP synthases can work in reverse to hydrolyze ATP and pump protons across the membrane to increase the membrane proton gradient (see end of video above).
The proton motive force drives protons through a channel in the ATP synthase, and turns the rotor at approx 100 rpm. The turning rotor changes the shape of the cytoplasmic subunits (called the F1 ATPase), which bind ADP and inorganic phosphate and bond them together to form ATP. Each 360 degree turn of the rotor results in synthesis of 3 ATP molecules.
This proton gradient is analogous to water stored in an elevated reservoir. The higher the water level in the reservoir, the more potential energy is available to accomplish mechanical work like turning a water wheel to grind grain. In the same way, the greater the difference in proton concentrations across the membrane, the more energy is available for ATP synthase to make ATP. Indeed, the ATP synthase complex even resembles a water wheel, in that the flow of protons down their concentration gradient, through ATP synthase, causes a part of ATP synthase to rotate.
The amount of energy released by these redox reactions, and thus the amount of energy available for ATP synthesis, depends on the redox potential of the terminal electron acceptor. Oxygen (O2) has the greatest redox potential, and thus results in the most ATP synthesized. Bacteria and Archaea can use other terminal electron acceptors with lower redox potential when oxygen is not available. This produces less ATP.