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Cytochrome b6/f complex from the cyanobacterium Synechocystis 6803: evidence of dimeric organization and identification of chlorophyll-binding subunit.
- Source :
-
FEBS letters [FEBS Lett] 1997 Sep 15; Vol. 414 (3), pp. 585-9. - Publication Year :
- 1997
-
Abstract
- Fractionation of photosynthetic membranes from the cyanobacterium Synechocystis 6803 by polyacrylamide gel electrophoresis in the presence of Deriphat-160 allowed the isolation of a number of pigmented bands. Two of them, with molecular masses of 240+/-20 and 110+/-15 kDa respectively, showed peroxidase activity and, by means of polypeptide composition, immunoblotting and N-terminal sequencing, were identified as dimeric and monomeric cytochrome b6/f complexes, containing 1.3+/-0.35 chlorophyll molecules per cytochrome f. Further fractionation of monomeric complexes by mild gel electrophoresis in the presence of sodium dodecyl sulfate indicated that it is the cytochrome b6 polypeptide which provides the actual binding site for the chlorophyll molecule observed in the complex.
- Subjects :
- Bacterial Proteins analysis
Bacterial Proteins chemistry
Cytochrome b6f Complex
Dimerization
Electrophoresis, Polyacrylamide Gel methods
Heme chemistry
Imidoesters chemistry
Immunoblotting
Indicators and Reagents chemistry
Iron-Sulfur Proteins analysis
Iron-Sulfur Proteins immunology
Spectrum Analysis methods
Chlorophyll metabolism
Cyanobacteria chemistry
Cytochrome b Group chemistry
Cytochrome b Group metabolism
Electron Transport Complex III
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 414
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 9323041
- Full Text :
- https://doi.org/10.1016/s0014-5793(97)01078-8