Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump.
A spectroscopic and functional analysis of two point-mutated bacteriorhodopsins (BRs) from phototrophic negative halobacterial strains is reported. Bacteriorhodopsin from strain 384 contains a glutamic acid instead of an aspartic acid at position 85 and BR from strain 326 contains asparagine instead...
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| 出版年: | EMBO J |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group
1989
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC401006/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2548851/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1989.tb03556.x |
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