Abstract
The use of lanthanide energy transfer in the "rapid-diffusion limit" for probing the electrostatic properties of proteins has been investigated by measuring rates of energy transfer from Tb(III) chelates (having charges 1+, 0, and 1-) to the heme of sperm whale met(aquo)myoglobin, as a function of pH. The results are in good agreement with the predictions of a simple model involving the overall charge of the protein. The preparation of terbium(III) N,N′-bis(2-hydroxyethyl)-ethylenediaminediacetate, a new positively charged Tb(III) chelate similar in size and shape to negative terbium(III) ethylenediaminetetraacetate and neutral terbium(III) N-(2-hydroxyethyl)ethylenediaminetriacetate, is described.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6247-6254 |
| Number of pages | 8 |
| Journal | Biochemistry |
| Volume | 22 |
| Issue number | 26 |
| State | Published - 1983 |
ASJC Scopus subject areas
- Biochemistry
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Wensel, T. G., & Meares, C. F. (1983). Electrostatic properties of myoglobin probed by diffusion-enhanced energy transfer. Biochemistry, 22(26), 6247-6254.