TY - JOUR
T1 - INTERACTIONS OF BOTH MELITTIN AND ITS SITE‐SPECIFIC MUTANTS WITH BACTERIORHODOPSIN OF Halobacterium halobium
T2 - SITES OF ELECI'ROSTATIC INTERACI'ION ON MELITI'IN
AU - Jiang, Qiu‐Xing ‐X
AU - Hu, Kun‐Sheng ‐S
AU - Shi, Hua
PY - 1994/8
Y1 - 1994/8
N2 - Abstract Melittin and its site‐specific mutants differentially delay the slow‐decaying component of the photocycle intermediate M412 of bacteriorhodopsin in the purple membrane and the acetylated purple membrane whose several lysine residues are modified. This effect is attributed to the interaction of the total positive charges of melittin or its mutants with the total negative charges of bacteriorhodopsin. The effects of melittin and its mutants on the Triton X‐100–solubilized bacteriorhodopsin monomers are somewhat complicated but are associated with their charges. These results show that there is electrostatic interaction between bacteriorhodopsin and melittin and that both N‐and C‐termini of melittin function as sites of the interaction, with Arg 22 and Arg 24 making a prominent contribution to the effective surface charge of melittin. Melittin, at certain concentrations, partially restores the decreased photoactivity of the bacteriorhodopsin monomers trapped in the Triton‐lipid‐protein mixed micelles, which suggests that melittin may compete with Triton X‐100 for the binding sites on the bacteriorhodopsin monomers. Other kinds of interactions between bacteriorhodopsin and melittin are also indicated. The possible states of melittin in membranes are discussed.
AB - Abstract Melittin and its site‐specific mutants differentially delay the slow‐decaying component of the photocycle intermediate M412 of bacteriorhodopsin in the purple membrane and the acetylated purple membrane whose several lysine residues are modified. This effect is attributed to the interaction of the total positive charges of melittin or its mutants with the total negative charges of bacteriorhodopsin. The effects of melittin and its mutants on the Triton X‐100–solubilized bacteriorhodopsin monomers are somewhat complicated but are associated with their charges. These results show that there is electrostatic interaction between bacteriorhodopsin and melittin and that both N‐and C‐termini of melittin function as sites of the interaction, with Arg 22 and Arg 24 making a prominent contribution to the effective surface charge of melittin. Melittin, at certain concentrations, partially restores the decreased photoactivity of the bacteriorhodopsin monomers trapped in the Triton‐lipid‐protein mixed micelles, which suggests that melittin may compete with Triton X‐100 for the binding sites on the bacteriorhodopsin monomers. Other kinds of interactions between bacteriorhodopsin and melittin are also indicated. The possible states of melittin in membranes are discussed.
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U2 - 10.1111/j.1751-1097.1994.tb05087.x
DO - 10.1111/j.1751-1097.1994.tb05087.x
M3 - Article
C2 - 7938217
AN - SCOPUS:0028485671
SN - 0031-8655
VL - 60
SP - 175
EP - 178
JO - Photochemistry and Photobiology
JF - Photochemistry and Photobiology
IS - 2
ER -