On the basis of its generally accessible I/II redox couple and bioavailability, copper plays a
wide variety of roles in nature that mostly involve electron transfer (ET), O 2 binding …

The field of bioinorganic chemistry is at a propitious stage of development. Ever more
complex metallobiomolecules are isolated and purified, physical methodologies and …

This is a sequel to the previous Perspective “The CH–π hydrogen bond in chemistry.
Conformation, supramolecules, optical resolution and interactions involving carbohydrates” …

Protein Radicals in Enzyme Catalysis. [Chem. Rev. 1998, 98, 705−762 | Chemical Reviews ACS
ACS Publications C&EN CAS Find my institution Log In Chemical Reviews ACS Publications …

Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …

In most organisms, the conversion of-D-galactose to the more metabolically useful glucose 1-
phosphate is accomplished by the action of four enzymes that constitute the Leloir pathway …

Although the number of proteins that utilize copper as an essential cofactor is not
exceptionally large, the roles played by many of these proteins appear central to the success …

Although Escherichia coli has long been recognized as the best-understood living organism,
little was known about its abilities to use aromatic compounds as sole carbon and energy …

A previously unknown redox cofactor has been identified in the active site of lysyl oxidase
from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra …

Background: The enzyme methylmalonyl-coenzyme A (CoA) mutase, an αβ heterodimer of
150 kDa, is a member of a class of enzymes that uses coenzyme B 12 (adenosylcobalamin) …