Details

Autor(en) / Beteiligte

• Quiroz, Soledad
• Kim, Jong K
• Mulrooney, Scott B
• Hausinger, Robert P
• Sigel, Roland K. O
• Sigel, Helmut
• Sigel, Astrid

Titel

Chaperones of Nickel Metabolism

Ist Teil von

• Nickel and Its Surprising Impact in Nature, 2007, p.519-544

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2007

Link zum Volltext

Quelle

Wiley-Blackwell Online Books - All Titles (includes Withdrawn titles)

Beschreibungen/Notizen

• Nickel is an essential micronutrient of many organisms where it serves as a cofactor for enzymes involved in several critical metabolic processes. Like other transition metal ions, however, excess Ni is toxic to cells; thus, synthesis of these Ni‐enzymes requires the presence of carefully controlled Ni‐processing mechanisms that range from selective transport of Ni into the cells to productive insertion of Ni into the apoproteins. Various accessory proteins participate in these processes and are required for the biosynthesis of several Ni‐dependent enzymes. Here, we provide brief overviews of the catalytic activities, biological roles, and active site architectures of eight structurally characterized Ni‐dependent enzymes. In addition, we summarize what is known about activation of these Ni‐enzymes and emphasize two particular accessory protein roles: metallochaperones that bind and deliver Ni to the apoprotein forms of the enzymes and molecular chaperones that ensure productive conformations of the apoproteins for Ni incorporation.