Tyrosine 162 of the photosynthetic reaction center L-subunit plays a critical role in the cytochrome c2 mediated rereduction of the photooxidized bacteriochlorophyll dimer in Rhodobacter sphaeroides. I: Site-directed mutagenesis and initial characterization
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Veröffentlicht in: | Biochemistry (Easton) 1993, Vol.32 (40), p.10885-10893 |
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container_title | Biochemistry (Easton) |
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creator | FARCHAUS, J. W WACHTVEITL, J MATHIS, P OESTERHELT, D |
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ispartof | Biochemistry (Easton), 1993, Vol.32 (40), p.10885-10893 |
issn | 0006-2960 1520-4995 |
language | eng |
recordid | cdi_pascalfrancis_primary_3797041 |
source | ACS Publications |
subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Molecular biophysics Photochemistry. Photosynthesis. Bioluminescence Radiation-biomolecule interaction |
title | Tyrosine 162 of the photosynthetic reaction center L-subunit plays a critical role in the cytochrome c2 mediated rereduction of the photooxidized bacteriochlorophyll dimer in Rhodobacter sphaeroides. I: Site-directed mutagenesis and initial characterization |
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