The complete amino acid sequence of the single light harvesting protein from chromatophores of Rhodospirillium rubrum G‐9⁺

The Complete Amino‐Acid Sequence of the Large BacteriochlorophyII‐Binding Polypeptide from Light‐Harvesting Complex II (B800—850) of Rhodopseudomonas capsulata

“…The observed difference in M , in dodecyl sulfate electrophoresis and sequence determination, respectively, may be due to the high hydrophobicity of this polypeptide (about 72 x), which allows some secondary structure in the presence of dodecyl sulfate, which influences the electrophoretic mobility. A similar effect has been observed with other bacteriochlorophyll-binding membrane proteins [6,17].…”

“…The amino acid sequence shows a hydrophobic stretch from residues 16 to 35 similar to that found in the amino acid sequence of the light-harvesting polypeptide of Rhodospirillum ruhrum, where the hydrophobic stretch was in the position 13-33 [17]. The C-terminal sequence (position 49-59) is hydrophobic while the N-terminal part is more hydrophilic.…”

“…However, two lysine residues at positions 5 and 11 will possibly give a positive charge to the N-terminal stretch and facilitate the contact of the N terminus to the membrane. Histidine in position 31 may be a candidate involved in the interaction between bacteriochlorophyll and protein as in the case of the light-harvesting polypeptide from R. ruhvum (His in position 29 [17]). It was reported that in the water-soluble light-harvesting bacteriochlorophyll-protein complex of the green phototrophic bacterium Prosthecochloris uerfuurii histidine residues interact with bacteriochlorophyll a [18].…”

“…It was reported that in the water-soluble light-harvesting bacteriochlorophyll-protein complex of the green phototrophic bacterium Prosthecochloris uerfuurii histidine residues interact with bacteriochlorophyll a [18]. 17'x of the amino acid residues of the M,-7322 polypeptide (light-harvesting complex B800-850 of Rhodopseudomonus capsulata) is homologous to the lightharvesting polypeptide (B870) of R. ruhrum [17].…”

“…This paper presents the coinplete amino acid sequence of the '10000-M, polypeptide' (large bacteriochlorophyllbinding polypeptide), which was proposed to be associated with 2 mol bacteriochlorophyll a giving the 855-nm absorption band [3,8]. The isolation and sequence analysis of this hydrophobic membrane polypeptide followed a strategy and technique which have been described recently from this laboratory [9,17].…”