title: [Role of bacteriochlorophyll in stabilization of the structure of the near-central and peripheral light-harvesting complexes from purple photosynthetic bacteria].
abstract: Pheophytinization of bacteriochlorophyll (BChl) at low pH was investigated in the core (LH1) and peripheral (LH2) light-harvesting complexes, as well as in the ensemble of the reaction center (RC) with the LH1 complex. The stages in disintegration of the native BChl forms in the LH1 complex and in its ensemble with RC were revealed. They were observed as emergence of the absorption band of monomeric BChl and an increase in its intensity, followed by its transformation into the band of monomeric bacteriopheophytin (BPh) and then into the band of aggregated BPh. Unlike the LH1 complex, in the case of the LH2 complex monomeric BChl was never detected as an intermediate product. While the spectra revealed formation of monomeric BPh, its accumulation did not occur, since its aggregation is very rapid compared to that in the LH1 complex and in the RC-LH1 ensemble. PAG electrophoresis revealed that pheophytinization of BChl in the LH2 complex was accompanied by disruption of the stable cylindrical structure of this complex with emergence of characteristic fragments consisting of α and β peptides and bearing monomeric BPh, as well as of the α peptide aggregates bearing BPh aggregates. Unlike the LH2 complex, BChl pheophytinization in the LH1 complex did not result in its fragmentation. This is an indication of different types of structural stabilization in the LH1 and LH2 complexes. In the LH2 complex, coordination of bacteriochlorophyll Mg2+ by conservative histidine residues of the α and β polypeptides is the main factor responsible for the maintenance of its cylindrical structure. Stability of the LH1 complex is probably based primarily on the highly specific hydrophobic interactions between the surfaces of individual polypeptide chains, since the presence of hydrogen bonds results in autonomy of each αβ3BChl2 subunit, rather than in stabilization of the LH1 complex as a whole.
authors.forename: A A
authors.initials: AA
authors.lastname: Solov'ev
authors.forename: Iu E
authors.initials: IuE
authors.lastname: Erokhin
mesh_terms: D001429:Bacteriochlorophylls / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability / Q000502:physiology; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism* / Q000648:ultrastructure; D012247:Rhodospirillum rubrum / Q000201:enzymology* / Q000648:ultrastructure
chemical_list: D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes