A Companion to Plant Physiology, Fifth Edition by Lincoln Taiz and Eduardo Zeiger
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Topic 7.11

Chlorophyll Biosynthesis

In the first phase of chlorophyll biosynthesis, the amino acid glutamic acid is converted to 5-aminolevulinic acid (ALA) (Web Figure 7.11.A). This reaction is unusual in that it involves a covalent intermediate in which the glutamic acid is attached to a transfer RNA molecule. This is one of a very small number of examples in biochemistry in which a tRNA is utilized in a process other than protein synthesis. Two molecules of ALA are then condensed to form porphobilinogen (PBG), which ultimately form the pyrrole rings in chlorophyll. The next phase is the assembly of a porphyrin structure from four molecules of PBG. This phase consists of six distinct enzymatic steps, ending with the product protoporphyrin IX.

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Web Figure 7.11.A   The biosynthetic pathway of chlorophyll. The pathway begins with glutamic acid, which is converted to 5-aminolevulinic acid (ALA). Two molecules of ALA are condensed to form porphobilinogen (PBG). Four PBG molecules are linked to form protoporphyrin IX. The magnesium (Mg) is then inserted, and the light-dependent cyclization of ring E, the reduction of ring D, and the attachment of the phytol tail complete the process. Many steps in the process are omitted in this figure. (Click image to enlarge.)

All the biosynthesis steps up to this point are the same for the synthesis of both chlorophyll and heme (see textbook Figures 7.27 and 7.28). But here the pathway branches, and the fate of the molecule depends on which metal is inserted into the center of the porphyrin. If magnesium is inserted by an enzyme called magnesium chelatase, then the additional steps needed to convert the molecule into chlorophyll take place; if iron is inserted, the species ultimately becomes heme.

The next phase of the chlorophyll biosynthetic pathway is the formation of the fifth ring (ring E) by cyclization of one of the propionic acid side chains to form protochlorophyllide. The pathway involves the reduction of one of the double bonds in ring D, using NADPH. This process is driven by light in angiosperms and is carried out by an enzyme called protochlorophyllide oxidoreductase (POR). Non-oxygen-evolving photosynthetic bacteria carry out this reaction without light, using a completely different set of enzymes. Cyanobacteria, algae, lower plants, and gymnosperms contain both the light-dependent POR pathway and the light-independent pathway. Seedlings of angiosperms grown in complete darkness lack chlorophyll, because the POR enzyme requires light. These etiolated plants very rapidly turn green when exposed to light. The final step in the chlorophyll biosynthetic pathway is the attachment of the phytol tail, which is catalyzed by an enzyme called chlorophyll synthetase (Malkin and Nyogi 2000).

The elucidation of the biosynthetic pathways of chlorophylls and related pigments is a difficult task, in part because many of the enzymes are present in low abundance. Recently, genetic analysis has been used to clarify many aspects of these processes (Suzuki et al. 1997, Armstrong and Apel 1998).

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