2Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
* To whom correspondence should be addressed.
Received December 17, 2018; Revised January 28, 2019; Accepted February 7, 2019
Studying pigment–protein interactions in the photosynthetic reaction centers (RCs) is important for the understanding of detailed mechanisms of the photochemical process. This paper describes spectral and photochemical characteristics, pigment composition, and stability of the Rhodobacter sphaeroides RCs with the I(L177)Y and I(M206)Y amino acid substitutions. The obtained data are compared with the properties of I(L177)H, I(L177)D, and I(M206)H RCs reported previously. It is shown that the I(L177)Y and I(M206)Y mutations cause a similar shift of the QYP band in the absorption spectra of the mutant RCs and do not affect the distribution of the electron spin density within the photo-oxidized P+ dimer. The differences in the position and amplitude of the QYB band in the I(L177)Y and I(M206)Y RCs were determined. The results indicate the possibility of new pigment–protein interactions in the vicinity of monomeric bacteriochlorophylls in the A and B chains, which might be of interest for future research.
KEY WORDS: Rhodobacter sphaeroides, photosynthetic reaction center, pigment–protein interactions, purple bacteria, site-directed mutagenesis