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. 2. Quantitative kinetic analysis

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10894-10904 ◽  
Author(s):  
J. Wachtveitl ◽  
J. W. Farchaus ◽  
P. Mathis ◽  
D. Oesterhelt
2017 ◽  
Vol 35 ◽  
pp. 103-111 ◽  
Author(s):  
Vincenzo De Leo ◽  
Lucia Catucci ◽  
A. Evelyn Di Mauro ◽  
Angela Agostiano ◽  
Livia Giotta ◽  
...  

2015 ◽  
Vol 1722 ◽  
Author(s):  
Rocco Roberto Tangorra ◽  
Alessandra Antonucci ◽  
Francesco Milano ◽  
Simona la Gatta ◽  
Alessandra Operamolla ◽  
...  

ABSTRACTOrganic biological hybrid systems, accessible by covalent functionalization of photosynthetic proteins with molecular antennas, represent a promising novelty to enhance natural photosynthesis. In this paper, we present the successful bioconjugation of a commercial fluorophore, fluorescein isothiocyanate (FITC), to the photosynthetic reaction center RC from the bacterium Rhodobacter sphaeroides strain R26. The resulting hybrid outperforms the pristine protein in hole-electron couple generation yield, exclusively at wavelengths where the fluorophore absorbs while the protein does not.


FEBS Letters ◽  
1989 ◽  
Vol 258 (1) ◽  
pp. 47-50 ◽  
Author(s):  
B. Arnoux ◽  
A. Ducruix ◽  
F. Reiss-Husson ◽  
M. Lutz ◽  
J. Norris ◽  
...  

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