The current state of knowledge on how copper metallochaperones support the maturation of
cuproproteins is reviewed. Copper is needed within mitochondria to supply the CuA and …

Metal ions, especially with high chemical activity (eg redox-active Cu and Fe) must be
carefully managed in biological systems. The “uncontrolled” activity, eg catalysis of Fenton …

Biological copper is coordinated predominantly by just three ligand types: the side chains of
histidine, cysteine, and methionine, with of course some exceptions. The arrangement of …

Copper (Cu) is an essential trace element for all living organisms and used as cofactor in
key enzymes of important biological processes, such as aerobic respiration or superoxide …

Eukaryotic cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial
respiratory chain. COX is a multimeric enzyme formed by subunits of dual genetic origin …

Metals are essential elements of all living organisms. Among them, copper is required for a
multiplicity of functions including mitochondrial oxidative phosphorylation and protection …

Human SCO1 and SCO2 are metallochaperones that are essential for the assembly of the
catalytic core of cytochrome c oxidase (COX). Here we show that they have additional …

In high-throughput genome-level protein investigation efforts, such as Structural Genomics,
the systematic experimental characterization of metal-binding properties (ie, the …

Copper is an essential but potentially harmful trace element required in many enzymatic
processes involving redox chemistry. Cellular copper homeostasis in mammals is …

The human protein Cox17 contains three pairs of cysteines. In the mitochondrial
intermembrane space (IMS) it exists in a partially oxidized form with two S–S bonds and two …