INTERACTIONS OF BOTH MELITTIN AND ITS SITE‐SPECIFIC MUTANTS WITH BACTERIORHODOPSIN OF Halobacterium halobium: SITES OF ELECI'ROSTATIC INTERACI'ION ON MELITI'IN

Qiu‐Xing ‐X Jiang, Kun‐Sheng ‐S Hu, Hua Shi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)175-178
Number of pages4
JournalPhotochemistry and Photobiology
Volume60
Issue number2
DOIs
StatePublished - 1994

Fingerprint

Halobacterium salinarum
Melitten
Bacteriorhodopsins
Ions
monomers
membranes
ions
interactions
Purple Membrane
lysine
Monomers
micelles
Membranes
electrostatics
Octoxynol
Micelles
Surface charge
Coulomb interactions
Static Electricity
Lysine

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Physical and Theoretical Chemistry

Cite this

INTERACTIONS OF BOTH MELITTIN AND ITS SITE‐SPECIFIC MUTANTS WITH BACTERIORHODOPSIN OF Halobacterium halobium : SITES OF ELECI'ROSTATIC INTERACI'ION ON MELITI'IN. / Jiang, Qiu‐Xing ‐X; Hu, Kun‐Sheng ‐S; Shi, Hua.

In: Photochemistry and Photobiology, Vol. 60, No. 2, 1994, p. 175-178.

Research output: Contribution to journalArticle

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abstract = "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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