Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin.
Recently, a number of aspartic acid mutants of bacteriorhodopsin have been shown to be defective in steady-state proton transport. Here we report time-resolved measurements of light-induced proton release and uptake for these mutants. Proton transfers between the protein and the aqueous phase were d...
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| Udgivet i: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
1989
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC286505/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2536166/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.2.529 |
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