ATP Production

In plants essentially all electron flow from water follows the pathway shown in Figure 3, at least up to ferredoxin. However, once an electron reaches ferredoxin the electron pathway becomes branched, enabling a fraction of the redox free energy to enter other pathways, including cycling through the Photosystem I reaction center. Photosystem I cyclic electron transport provides additional energy for ATP production, which allows plants to adjust the energy flow according to their metabolic needs.

Most of the energy from the electron transfer reactions is stored as redox energy in NADPH as described above. However, some of the energy

is stored across the membrane of the photosynthetic vesicle in the form of a pH gradient (or protein gradient) and an electric potential (positive inside). As previously noted, the electron transport chain concentrates protons in the inner water phase of the vesicle by the release of protons during the oxidation of water by Photosystem II and by transporting protons from the outer water phase to the inner water phase via plastoquinone (Figure 3). In addition, electron transport creates a net positive charge on the inner side and a net negative charge on the outer side of the vesicle, which gives rise to an electric potential across the membrane. The energy stored in the pH gradient and electric potential is known as the transmembrane proton electrochemical potential or the proton motive force.

The conversion of proton electrochemical energy into the chemical-free energy of ATP is accomplished by a single protein complex known as ATP synthase, which catalyzes the formation of ATP by the addition of inorganic phosphate (P.) to ADP:

The reaction is energetically uphill and is driven by the transmembrane proton electrochemical gradient. The ATP synthase enzyme is a molecular rotary motor. Protons move through a channel in the ATP synthase pro-

pH a measure of acidity or alkalinity; the pH scale ranges from 0 to 14, with 7 being neutral; low pH numbers indicate high acidity; high numbers indicate alkalinity

Figure 4: Rotary model of how ATP synthase catalyzes ATP. Redrawn from Fillingame, 1999, pp. 1687-88.

genome the genetic material of an organism

tein (from the inner water phase to the outer water phase of the vesicle) providing the energy for ATP synthesis. However, the protons are not involved in the chemistry of adding phosphate to ADP at the catalytic site. Although it has not been proven, it appears that proton flow drives the rotation part of the ATP synthase at rates as high as one hundred revolutions per second (Figure 4). The rotation of ATP synthase can be thought of as pushing ADP and Pi together to form ATP and water.

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