SciCombinator

Discover the most talked about and latest scientific content & concepts.

Abstract
The interplay between redox-active transition metal ions and redox-active ligands in metalloenzyme sites is an area of considerable research interest. Galactose oxidase (GO) is the archetypical example, catalyzing the aerobic oxidation of primary alcohols to aldehydes via two one-electron cofactors: a copper atom and a cysteine-modified tyrosine residue. The electronic structure of the oxidized form of the enzyme (GO(ox)) has been investigated extensively through small molecule analogues including metal-salen phenoxyl radical complexes. Similar to GO(ox), one-electron oxidized metal-salen complexes are mixed-valent species, in which molecular orbitals (MOs) with predominantly phenolate and phenoxyl π-character act as redox-active centers bridged by mixing with metal d-orbitals. A detailed evaluation of the electronic distribution in these odd electron species using a variety of spectroscopic, electrochemical, and theoretical techniques has led to keen insights into the electronic structure of GO(ox).
Tweets*
0
Facebook likes*
0
Reddit*
0
News coverage*
0
Blogs*
0
SC clicks
0
Concepts
Transition metal, Iron, Redox, Electron, Alcohol, Atom, Electron configuration, Molecule
MeSH headings
-
comments powered by Disqus

* Data courtesy of Altmetric.com