Substitution of isoleucine L177 by histidine inRhodobacter sphaeroidesreaction center results in the covalent binding of PAbacteriochlorophyll to the L subunit

Author:

Fufina Tatiana Y.,Vasilieva Lyudmila G.,Khatypov Ravil A.,Shkuropatov Anatoly Ya.,Shuvalov Vladimir A.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference14 articles.

1. X-ray structure analysis of a membrane protein complex electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis;Deisenhofer;J. Mol. Biol.,1984

2. M.R. Wasielewski Energy and Electron Transfer in Covalently Linked Chlorophyll – Containing Donor–Acceptor Molecules H. Scheer Chlorophylls 1991 CRC Press Boca Raton 269 286

3. C.R.D. Lancaster H. Michel Photosynthetic Reaction Centers of Purple Bacteria A. Messerschmidt R. Huber T. Poulos K. Wieghardt Handbook of Metalloproteins 2001 John Wiley & Sons, Ltd Chichester 119 135

4. Substitution of isoleucine L177 by histidine affects the pigment composition and properties of the reaction center of the purple bacterium Rhodobacter sphaeroides;Khatypov;Biochemistry (Moscow),2005

5. Construction and characterization of a mutant of Rhodobacter sphaeroides with the reaction center as the sole pigment–protein complex;Jones;Biochemistry,1992

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