Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a
protein, affect the nuclei in their surrounding in various ways. One of these effects is the …

Copper is widely used in nature to promote electron transfer in a variety of processes. The
metal is usually found as a mononuclear type 1 copper site protected by a protein envelope …

The evaluation of reduction potentials of proteins by ab initio approaches presents a major
challenge for computational chemistry. This is addressed in the present investigation by …

The relative Cu2+/Cu+ reduction potentials of six type-1 copper sites (cucumber
stellacyanin, P. aeruginosa azurin, poplar plastocyanin, C. cinereus laccase, T. ferrooxidans …

Expressed protein ligation was used to replace the axial methionine of the blue copper
protein azurin from Pseudomonas aeruginosa with unnatural amino acids. The highly …

In an effort to characterize the roles of each metal ion in metallo-β-lactamase NDM-1,
heterodimetallic analogues (CoCo-, ZnCo-, and CoCd-) of the enzyme were generated and …

Cupredoxins are small proteins that contain type I copper centers, which are ubiquitous in
nature. They function as electron transfer shuttles between proteins. This review of the …

▪ Abstract The review deals with recent advances in magnetic resonance spectroscopy (hf
EPR and NMR) of paramagnetic metal centers in biological macromolecules. In the first half …

The key to type 1 copper (T1Cu) function lies in the fine tuning of the CuII/I reduction
potential (E°′ T1Cu) to match those of its redox partners, enabling efficient electron transfer …

Motivated by the ambition to establish an enzyme-driven bioleaching pathway for copper
extraction, properties of the Type-1 copper protein rusticyanin from Acidithiobacillus …