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Oxidative switches in functioning of mammalian copper chaperone Cox17.

• Anastassia Voronova, Wolfram Meyer-Klaucke, +5 authors Peep Palumaa
• The Biochemical journal
• 2007

Cox17, a copper chaperone for cytochrome-c oxidase, is an essential and highly conserved protein in eukaryotic organisms. Yeast and mammalian Cox17 share six conserved cysteine residues, which are… (More)

Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase.

• Peep Palumaa, Liina Kangur, Anastassia Voronova, Rannar Sillard
• The Biochemical journal
• 2004

Cox17, a copper chaperone for cytochrome c oxidase, is an essential and highly conserved protein. The structure and mechanism of functioning of Cox17 are unknown, and even its metalbinding… (More)

Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents.

• Anastassia Voronova, Jekaterina Kazantseva, Marina Tuuling, Niina Sokolova, Rannar Sillard, Peep Palumaa
• Protein expression and purification
• 2007

Copper chaperone for cytochrome c oxidase (Cox17) is a 7 kDa copper-binding protein, which facilitates incorporation of copper ions into Cu(A) site of cytochrome c oxidase. Cox17 contains six… (More)

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