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pH-dependence of interaction between melittin and bacteriorhodopsin

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【作者】 蒋秋兴胡坤生王玮

【Author】 JIANG Qiuxing HU Kunsheng and WANG Wei(Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China)

【机构】 Institute of BiophysicsChinese Academy of SciencesBeijing 100101ChinaChina

【摘要】 <正> Melittin differentially slowed down the fast (M412f) and the slow (M412s) decay components of the photocyde intermediate M of trimeric bacteriorhodopsin in purple membrane while it accelerated the M412s of Triton X-100-solubilized bacteriorhodopsin monomers. Raising the bulk pH could enhance the effect of melittin on the M412s of bacteriorhodopsin in these two states. From pH 5.5 to 8.8, melittin slightly influenced the yield of intermediate M in purple membrane, whereas the yield of M412s decreased and subsequently reversed with the addition of melittin. Moreover, the monomeric bacteriorhodopsin bleached more readily in the presence of melittin and the higher pH made the bleaching effect of melittin more intensive as well. These results re-certify our former suggestions that there was electrostatic interaction between melittin and bacteriorhodopsin, and indicate that the biphasic M decay may not result from the well-known linear kinetic scheme (M→N →BR). At last the mechanisms underlying the interact

【Abstract】 Melittin differentially slowed down the fast (M412f) and the slow (M412s) decay components of the photocyde intermediate M of trimeric bacteriorhodopsin in purple membrane while it accelerated the M412s of Triton X-100-solubilized bacteriorhodopsin monomers. Raising the bulk pH could enhance the effect of melittin on the M412s of bacteriorhodopsin in these two states. From pH 5.5 to 8.8, melittin slightly influenced the yield of intermediate M in purple membrane, whereas the yield of M412s decreased and subsequently reversed with the addition of melittin. Moreover, the monomeric bacteriorhodopsin bleached more readily in the presence of melittin and the higher pH made the bleaching effect of melittin more intensive as well. These results re-certify our former suggestions that there was electrostatic interaction between melittin and bacteriorhodopsin, and indicate that the biphasic M decay may not result from the well-known linear kinetic scheme (M→N →BR). At last the mechanisms underlying the interaction of melittin with purple membranes and bacteriorhodopsin monomers are analyzed.

【基金】 Project supported by the National Natural Science Foundation of China and Grant for Key Project from the Chinese Academy of Sciences.
  • 【文献出处】 Science in China(Series C:Life Sciences) ,中国科学(C辑:生命科学)(英文版) , 编辑部邮箱 ,1996年04期
  • 【分类号】Q592
  • 【下载频次】10
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