We have performed low-temperature Stark spectroscopy on a variety of different LH2 complexes from four photosynthetic bacteria, with the aim of characterizing the electric field response of the B800 and B850 absorption properties as a function of the protein environment. The following LH2 complexes were investigated : B800-850 and B800-820 of Rhodopseudomonas (Rps) acidophila; B800-850, B800-840 (alpha Tyr(+13)-->Phe), and B800-826 (alpha Tyr(+13)-->Phe, alpha Tyr(+14)-->Leu) of Rhodobacter (Rb.) sphaeroides; B800-850 and B800-830 (obtained at high LDAO) of Ectothiorhodospira sp.; and B800-850 of Rhodospirillum (Rsp.) molischianum. For all these cases the spectral blue shift of B850 has been assigned to the loss hydrogen-bonding interaction with the acetyl carbonyl of bacteriochlorophyll a. Delta mu values for the 850 nm bands as well as for the blue-shifted bands are all on the order of 3-4.5 D/f. The loss of hydrogen-bonding interactions has only small effects on Delta mu in these complexes. The values of the difference polarizability, Tr(Delta alpha), are large (600-1400 Angstrom(3)/f(2)). The results are discussed in terms of crystal-structure-based models for LH2, in which pigment-pigment and pigment-protein interactions are considered; strong pigment-pigment interactions were found to be especially important. The values of Delta mu for the 800 nm band are small, 1.0-1.5 D/f for LH2 complexes from Rb. sphaeroides and Rps. acidophila. However, in Rsp. molischianum and Ectothiorhodospira sp. Delta mu values are much larger, of the order of 3 D/f. The difference in the B800 band is assigned to the difference in orientation of the B800 pigments in Rsp. molischianum and Ectothiorhodospira sp., as compared to the Rps. acidophila and Rb. sphaeroides. Due to the difference in orientation, the interactions of the Bchl a with the surrounding protein and neighboring carotenoid pigments are also not identical.