Cargando…
A Copper Cage‐Complex as Mimic of the pMMO Cu(C) Site
The active site of particulate methane monooxygenase (pMMO) and its mechanism of action are not known. Recently, the Cu(C) site emerged as a potential active site, but to date it lacks any study on biomimetic resemblance of the coordination environment provided by the enzyme. Here, the synthesis of...
Autores principales: | Bete, Sarah C., May, Leander K., Woite, Philipp, Roemelt, Michael, Otte, Matthias |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9544873/ https://www.ncbi.nlm.nih.gov/pubmed/35731651 http://dx.doi.org/10.1002/anie.202206120 |
Ejemplares similares
-
Synthesis of an Fe(terpy-cage)(2) dumbbell
por: Dournel, Frederic, et al.
Publicado: (2022) -
Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants
por: Spatola Rossi, Tatiana, et al.
Publicado: (2023) -
Stacking of a Cofacially
Stacked Iron Phthalocyanine
Dimer on Graphite Achieved High Catalytic CH(4) Oxidation
Activity Comparable to That of pMMO
por: Yamada, Yasuyuki, et al.
Publicado: (2023) -
Heteroleptic Ligation by an endo‐Functionalized Cage
por: Bete, Sarah C., et al.
Publicado: (2021) -
Suppression of Pepper mild mottle virus (PMMoV) by Modified Whey Proteins
por: Elsharkawy, Mohsen Mohamed, et al.
Publicado: (2022)