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Specific mutagenesis of a chlorophyll-binding protein. [Synechocystis]

Technical Report ·
OSTI ID:5671692

Chlorophyll, absorbing light energy for use in photosynthesis, is bound by specific proteins in thylakoid membranes such as CP47. His residues have been suggested to serve as chlorophyll ligands. To test the necessity of His residues in CP47, specific His residues have been altered to Tyr or Asn, and the effects of these mutations are now studied in vivo in the cyanobacterium Synechocystis sp. PCC 6803. Most mutations lead to a decreased photoautotrophic growth rate of the cyanobacterium, due in part to a decreased stability of the photosystem 2 complex. The effective relative antenna size of photosystem 2 in the various CP47 mutants is now being measured. The CP47 protein may also be involved in events at the donor side of photosystem 2. We have identified a region which can be deleted without obvious ill effects, and a domain which appears crucial for photosystem 2 structure and function. Residues of particular importance will be defined by further mutagenesis experiments. 1 fig., 1 tab.

Research Organization:
Arizona State Univ., Tempe, AZ (United States). Dept. of Botany
Sponsoring Organization:
DOE; USDOE, Washington, DC (United States)
DOE Contract Number:
FG02-89ER14031
OSTI ID:
5671692
Report Number(s):
DOE/ER/14031-3; ON: DE91014813
Country of Publication:
United States
Language:
English