Substitution of the mononuclear, non-heme iron cofactor in lipoxygenases for structural studies.
| Autor: | Jakobowski A; Department of Chemistry, East Carolina University, Greenville, NC, United States., Hill SG; Department of Chemistry, East Carolina University, Greenville, NC, United States., Guy SW; Department of Chemistry, East Carolina University, Greenville, NC, United States., Offenbacher AR; Department of Chemistry, East Carolina University, Greenville, NC, United States. Electronic address: offenbachera17@ecu.edu. |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | Methods in enzymology [Methods Enzymol] 2024; Vol. 704, pp. 59-87. Date of Electronic Publication: 2024 Jun 18. |
| DOI: | 10.1016/bs.mie.2024.05.011 |
| Abstrakt: | This Chapter describes methods for the biosynthetic substitution of the mononuclear, non-heme iron in plant and animal lipoxygenases (LOXs). Substitution of this iron center for a manganese ion results in an inactive, yet faithful structural surrogate of the LOX enzymes. This metal ion substitution permits structural and dynamical studies of enzyme-substrate complexes in solution and immobilized on lipid membrane surfaces. Representative procedures for two LOXs, soybean lipoxygenase (SLO) from plants and human epithelial 15-lipoxygenase-2 (15-LOX-2) from mammals, are described as examples. (Copyright © 2024. Published by Elsevier Inc.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|