Chlorophyll b inhibits the formation of photosystem I trimer in Synechocystis sp. PCC6803
Soichirou Satoh, Ayumi Tanaka
Abstract
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Soichirou Satoh, Ayumi Tanaka
Abstract
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Chlorophyllide a oxygenase (CAO) catalyzes two-step oxygenation reactions and converts chlorophyllide a to chlorophyllide b. When CAO was introduced into the Synechocystis sp. PCC6803 genome, chlorophyll b was synthesized and incorporated into P700-chlorophyll a-protein complexes. Curve analysis of photosystem I particles showed that Ca687 was decreased with a concomitant increase in Cb652 suggesting that chlorophyll b was incorporated into Ca687-binding sites. When the level of chlorophyll b was high, Ca704, which is known as red chlorophyll and photosystem I trimers were decreased. Formation of photosystem I trimers is discussed in relation to red chlorophyll and chlorophyll b accumulation.
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Chlorophyllide a oxygenase (CAO) catalyzes two-step oxygenation reactions and converts chlorophyllide a to chlorophyllide b. When CAO was introduced into the Synechocystis sp. PCC6803 genome, chlorophyll b was synthesized and incorporated into P700-chlorophyll a-protein complexes. Curve analysis of photosystem I particles showed that Ca687 was decreased with a concomitant increase in Cb652 suggesting that chlorophyll b was incorporated into Ca687-binding sites. When the level of chlorophyll b was high, Ca704, which is known as red chlorophyll and photosystem I trimers were decreased. Formation of photosystem I trimers is discussed in relation to red chlorophyll and chlorophyll b accumulation.
Key concepts: P700, Photosystem I, Chlorophyll, Chlorophyll a, Light-harvesting complexes of green plants, Photosystem II, Trimer, Chlorophyll b