cODH CHNHa 5-Aminolevulinic acid (ALA) Porphobilinogen《PBG COOH COOH NADPH, light Protochlorophyllide oxidoreductase chlorophyllide a Monovinyl protochlorophyllide a Phvtol tail Phytol tail Figure 3-8 Chlorophyll a
Figure 3-8
Light hI Xanthophyll Carotene ChIb DPA Reaction centre H2○ Figure 3-9 Primary reaction NADP
Figure 3-9 Primary reaction
STROMA Thylakoid Figure 3-9-1 0是08mp ra LUMEN FIGURE 7. 18 Organization of the protein complexes of the thy lakoid membrane Photosystem Il is located predominantly in the stacked regions of the thylakoid membrane; photosystem I and ATP synthase are found in the unstacked regions protruding into the stroma Cytochrome b, f complexes are evenly distributed. This LHC PSll Cytochrome PSI ATP synthase lateral separation of the two photosystems requires that electrons trimer b6f dimer and protons produced by photosystem Il be transported a consid erable distance before they can be acted on by photosystem I and the ATP-coupling enzyme (After Allen and Forsberg 2001)
Figure 3-9-1
-2.0 P700° ⑤ A gure -15 Fd NR -1.0 P680° 05 Pheo ③ Cytochrom NADPH Qa bf complex Cyt b Cyt b Fes 05 0 c→p(p0 evolving complex P680 Lg 02+H Photosystem II Photosystem
Figure 3-10
Stroma Figure 3-10-1 D2 DI CP43b559 CP47 Pheo Pheo P680 D h MSP (Mn (Mn) Lumen n Mn 2 H,O O2+4① Figure 12.12 Structural model of the PSll reaction center, a schematic representation showing the structure dominated by the two PSII reaction center proteins DI and D2. The model is based on analogies with the bacterial reaction center complex(see Fig 12.10).Electrons are transferred from P680 to pheophytin(Pheo)and subsequent y to two plastoquinone molecules, QA and QB. P680 is reduced by Z, a tyrosine residue in the DI subunit. The oxidation of water by the Mn cluster is also indi- cated. CP43 and CP47, chlorophyll a-binding proteins. DI is susceptible to photo- chemical damage and undergoes active turnover(see Chapter 14; Box 9.6)
Figure 3-10-1