Substitution of isoleucine L177 by histidine in Rhodobacter sphaeroides reaction center results in the covalent binding of PA bacteriochlorophyll to the L subunit
| Autor: | Anatoly Ya. Shkuropatov, L. G. Vasilieva, R. A. Khatypov, T. Y. Fufina, Vladimir A. Shuvalov |
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| Rok vydání: | 2007 |
| Předmět: |
Photosynthetic reaction centre
Models Molecular Stereochemistry Photosynthetic Reaction Center Complex Proteins Biophysics Covalent Interaction Rhodobacter sphaeroides Photochemistry Biochemistry Electron Transport chemistry.chemical_compound Structural Biology Genetics Histidine Bacteriochlorophyll Site-directed mutagenesis pigment–protein binding Isoleucine Molecular Biology Bacteriochlorophylls biology Chemistry Temperature Cell Biology Pigments Biological biology.organism_classification Photosynthetic reaction center Protein Subunits Amino Acid Substitution Covalent bond Spectrophotometry Photosynthetic membrane Electrophoresis Polyacrylamide Gel Protein Binding |
| Zdroj: | FEBS letters. 581(30) |
| ISSN: | 0014-5793 |
| Popis: | In this work, we report the unique case of bacteriochlorophyll (BChl) – protein covalent attachment in a photosynthetic membrane complex caused by a single mutation. The isoleucine L177 was substituted by histidine in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides. Pigment analysis revealed that one BChl molecule was missing in the acetone–methanol extract of the I(L177)H RCs. SDS–PAGE demonstrated that this BChl molecule could not be extracted with organic solvents apparently because of its stable covalent attachment to the mutant RC L-subunit. Our data indicate that the attached bacteriochlorophyll is one of the special pair BChls, PA. The chemical nature of this covalent interaction remains to be identified. |
| Databáze: | OpenAIRE |
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