Chlorophyll b inhibits the formation of photosystem I trimer in Synechocystis sp. PCC6803

FEBS Lett. 2002 Sep 25;528(1-3):235-40. doi: 10.1016/s0014-5793(02)03320-3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Chlorophyll / metabolism*
  • Chlorophyll A
  • Chlorophyllides / metabolism
  • Cyanobacteria / genetics
  • Cyanobacteria / metabolism*
  • Genes, Bacterial
  • Mutation
  • Oxygenases / genetics
  • Oxygenases / metabolism
  • Photosynthetic Reaction Center Complex Proteins / biosynthesis*
  • Photosynthetic Reaction Center Complex Proteins / chemistry*
  • Protein Structure, Quaternary
  • Spectrophotometry

Substances

  • Chlorophyllides
  • Photosynthetic Reaction Center Complex Proteins
  • Chlorophyll
  • chlorophyllide b
  • chlorophyll b
  • Oxygenases
  • chlorophyll a oxygenase
  • Chlorophyll A