Mutant reaction centers of Rhodobacter sphaeroides I(L177)H with strongly bound bacteriochlorophyll a: Structural properties and pigment-protein interactions

Methods of photoinduced Fourier transform infrared (FTIR) difference spectroscopy and circular dichroism were employed for studying features of pigment-protein interactions caused by replacement of isoleucine L177 by histidine in the reaction center (RC) of the site-directed mutant I(L177)H of Rhodo...

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Veröffentlicht in:	Biochemistry (Moscow) 2009, Vol.74 (1), p.68-74
Hauptverfasser:	Zabelin, A. A, Fufina, T. Y, Vasilieva, L. G, Shkuropatova, V. A, Zvereva, M. G, Shkuropatov, A. Y, Shuvalov, V. A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Amino acids Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriochlorophyll A - chemistry Bacteriochlorophyll A - metabolism Bacteriochlorophylls - metabolism Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Circular Dichroism Fourier transforms Life Sciences Microbiology Mutagenesis, Site-Directed Mutant Proteins - chemistry Mutant Proteins - isolation & purification Mutant Proteins - metabolism Mutants Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins - chemistry Photosynthetic Reaction Center Complex Proteins - genetics Photosynthetic Reaction Center Complex Proteins - metabolism Pigments Pigments, Biological - chemistry Pigments, Biological - metabolism Rhodobacter sphaeroides Rhodobacter sphaeroides - metabolism Spectroscopy, Fourier Transform Infrared Spectrum analysis
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