Back to Search
Start Over
The primary structure of the presumable BChl d-binding polypeptide of Chlorobium vibrioforme f. thiosulfatophilum
- Source :
- Zeitschrift fur Naturforschung. C, Journal of biosciences. 45(7-8)
- Publication Year :
- 1990
-
Abstract
- In addition to the previous isolated and sequenced polypeptides from green photosynthetic sulfur bacteria, which are presumably involved in binding BChl c and e, an analogous poly- peptide has been purified from the BChl d-containing bacterium Chlorobium vibrioforme f. thiosulfatophilum. The primary structure of this 6.15 kDa polypeptide was determined. It shows an extremely high homology (98.3%) to the corresponding polypeptide from Pelodictyon luteolum, indicative of an important functional role.
- Subjects :
- biology
Molecular Sequence Data
Photosynthetic Reaction Center Complex Proteins
Protein primary structure
Light-Harvesting Protein Complexes
chemistry.chemical_element
Pelodictyon luteolum
Chlorobium
Photosynthesis
biology.organism_classification
Sulfur
Chromatiaceae
General Biochemistry, Genetics and Molecular Biology
Molecular Weight
Biochemistry
chemistry
Bacterial Proteins
Sequence Homology, Nucleic Acid
Amino Acid Sequence
Peptide sequence
High homology
Bacteria
Chromatography, High Pressure Liquid
Subjects
Details
- ISSN :
- 09395075
- Volume :
- 45
- Issue :
- 7-8
- Database :
- OpenAIRE
- Journal :
- Zeitschrift fur Naturforschung. C, Journal of biosciences
- Accession number :
- edsair.doi.dedup.....1abfcedc2d08b0487ed8fba979eed37f