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4Photophosphorylation and ATP synthesis During photosynthetic electron transfer from water to NADP+, energy captured in two photoacts is stored as an electrochemical potential gradient of protons.

First, such reduction of QB requires protonation with protons drawn from the stromal side of the membrane. Reoxidation (and deprotonation) occurs towards the thylakoid lumen. In addition, protons are lost from the stromal side via protonation of reduced NADP and they are also cheap sunglasses oakley generated in the lumen during photolysis. A massive pH, of approximately 3 pH units, equivalent to an H+ ion concentration difference of three to four orders of magnitude, develops across the thylakoid membrane. This immense gradient drives ATP synthesis (catalysed by ATP synthase) within a large best oakley eyeglasses energy transducing complex embedded in the thylakoid membrane (Figure 1.11). ATP synthesis in chloroplasts (photophosphorylation) proceeds according to a mechanism that is basically similar to that in mitochondria. Chemiosmotic coupling (Mitchell 1961) which links the movement of protons down an electro chemical potential gradient to ATP synthesis via an ATP synthase applies in both organelles. However, the orientation of ATP synthase is opposite. In chloroplasts protons accumulate in thylakoid lumen and pass outwards through the ATP synthase into the stroma. In mitochondria, protons accumulate within the intermembrane space and move inwards, generating ATP and oxidising NADH within the matrix of these organelles (Figure 2.24). In chloroplasts, ATP synthase is called the CF0CF1 complex. The CF0 unit is a hydrophobic transmembrane multiprotein complex which contains a water filled proton conducting channel. The CF1 unit is a hydrophilic peripheral membrane protein complex that protrudes into the stroma. It contains a reversible ATPase and a gate which controls proton movement between CF0 and CF1. Entire CF0CF1 complexes are restricted to non appressed portions of thylakoid membranes due to their bulky CF1 unit. Direct evidence for ATP synthesis due to a transthylakoid pH gradient can be adduced as follows. a proton rich medium), thylakoid lumen equilibrate to this pH. If the chloroplasts, still in the dark, are rapidly transferred to a pH 8.0 buffer containing ADP and Pi, ATP synthesis then occurs. This outcome confirms a central role for the proton concentration difference between thylakoid lumen and stroma for ATP synthesis in vitro; but does such a process operate on that scale in vivo? Mordhay Avron, based in Israel, answered this question in part during the early 1970s via a most elegant approach (Rottenberg et al. 1972). Working with thylakoid preparations, Avron and colleagues established that neutral amines were free to exchange between bathing medium and thylakoid lumen, but once protonated in illuminated preparations they became trapped inside. By titrating the loss of such amines from the external oakley a frame sunglasses medium when preparations where shifted from dark to light, they were able to infer the amount retained inside. Knowing that the accumulation of amine depended upon H+ ion concentration in that lumen space, the difference in H+ ion concentration and hence pH across the membrane were established. At saturating light, chloroplasts generate a proton gradient of approximately 3.5 pH units across their thylakoid membranes. Protons for this gradient are derived from the oxidation of water molecules occurring towards the inner surface of PSII and from transport of four electrons through the Cyt b/f complex, combined with cotranslocation of eight protons from the stroma into the thylakoid space for each pair of water molecules oxidised. Electrical neutrality is main tained by the passage of Mg2+ and Cl across the membrane, and as a consequence there is only a very small electrical gradient across the thylakoid membrane. The electrochemical potential gradient that yields energy is thus due almost entirely to the concentration of intrathylakoid H+ ions. For every three protons translocated via ATP synthase, one ATP is synthesised. Linear electron transport therefore generates about four molecules of ATP per O2 evolved. Thus eight photons are absorbed for every four ATP molecules generated or for each O2 generated. Cyclic electron transport is slightly more efficient at producing ATP and generates about four ATP per six photons absorbed. However, linear electron transport also generates NADPH, which is equivalent, in energy terms, to six ATP per O2 released. As implied in Figure 1.11, the four thylakoid complexes, PSII, PSI, Cyt b/f and ATP synthase, are not evenly distributed in plant thylakoid membranes but show a lateral heterogeneity. This distribution is responsible for the highly characteristic structural organisation of the continuous thylakoid membrane into two regions, one consisting of closely appressed membranes or granal stacks, the other of non appressed stroma lamellae where outside surfaces of thylakoid membranes are in direct contact with the stroma. This structural organisation is shown on a modest scale in Figure 1.7, but extreme examples are evident in chloroplasts of shade adapted species grown in low light (Chapter 12). Under such conditions, membrane regions with clusters of PSII complexes and Cyt b/f complexes become appressed into classical granal stacks.

Cyt b/f complexes are present inside these granal stacks as well as in stroma lamellae, but PSI and ATP synthase are oakley store sunglasses absent from granal stacks. Linear electron transport occurs in granal stacks from PSII in appressed domains to PSI in granal margins. Nevertheless, shade plants have only a low rate of linear electron transport because they have fewer Cyt b/f and to a lesser extent fewer PSII complexes compared to PSI, a consequence of investing more chlorophyll in each PSII to enhance light harvesting (see Anderson (1986) and Chapter 12 for more detail).


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