High-resolution solution NMR spectra have been obtained for bacteriochlorophyll (BChl) a molecules in a biologically functional subunit of a bacterial core light-harvesting complex based on a modified reconstitution method. The reconstituted subunit of pigment-integral membrane polypeptides is stable and homogeneous at high concentrations at room temperature and exhibits a Q(y) absorption peak at 818 nm. H-1 and C-13 chemical shifts have been specifically assigned for BChl a using the fully and selectively C-13-labeled pigments incorporated with natural abundance polypeptides in deuterated detergent solution, Remarkable signal broadening has been observed upon reconstitution, where the bacteriochlorin macrocycle is shown in a highly restricted molecular motion while the phytol side chain remains relatively mobile, Two sets of resonances are revealed for 3(2), 8(1), 1(0), 12(1), and 13(4) protons, and 8(2) methyl protons exhibit four resonances with large upfield complexation shifts. The result indicates a nonequivalent state for the two BChl a molecules in the subunit and can be best interpreted in terms of a parallel face-to-face configuration with partial overlap over the pyrrolic rings II, III, and V. In comparison with BChl a in acetone, 8(2), 13(2), and 13(4) protons are largely perturbed, and the propionic and phytol side chain may adopt a different conformation in the reconstituted subunit. The C-13 chemical shift of 3(1) carbonyl carbon shows a large change downfield, indicating strong hydrogen bonding for all the acetyl carbonyls. Carbonyl carbons at 13(1) give rise to two C-13 resonances with equal intensities, suggesting that the keto carbonyl in one BChl a molecule within a subunit forms a stronger hydrogen bond than that in another BChl a molecule.