Bacteriopheophytin a in the active branch of the reaction center of rhodobacter sphaeroides is not disturbed by the protein matrix as shown by 13C photo-CIDNP MAS NMR

Published: Friday, 21 June 2013 - 14:00 UTC


Sai Sankar Gupta, K.B., et al., Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter sphaeroides Is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR. The Journal of Physical Chemistry B, 2013. 117(12): p. 3287-3297.

The electronic structure of bacteriopheophytin a (BPhe a), the primary electron acceptor (PhiA) in photosynthetic reaction centers (RCs) of the purple bacterium Rhodobacter sphaeroides, is investigated by photochemically induced dynamic nuclear polarization (photo-CIDNP) magic-angle spinning (MAS) NMR spectroscopy at atomic resolution. By using various isotope labeling systems, introduced by adding different (13)C selectively labeled delta-aminolevulinic acid precursors in the growing medium of R. sphaeroides wild type (WT), we were able to extract light-induced (13)C NMR signals originating from the primary electron acceptor. The assignments are backed by theoretical calculations. By comparison of these chemical shifts to those obtained from monomeric BPhe a in solution, it is demonstrated that PhiA in the active branch appears to be electronically close to free bacteriopheophytin. Hence, there is little effect of the protein surrounding on the cofactor functionally which contributes with its standard redox potential to the electron transfer process that is asymmetric.