The heme-copper oxidase superfamily shares a Zn2+-binding motif at the entrance to a proton pathway

作者：Lee Hyun Ju; Adelroth Pia^*

来源：FEBS Letters, 2013, 587(6): 770-774.

DOI：10.1016/j.febslet.2013.01.069

• cbb(3)
• Proton transfer
• K-pathway
• Nickel
• Liposome
• Nitric oxide reductase

Heme-copper oxidases (HCuOs) catalyse the reduction of oxygen, using the liberated free energy to maintain a proton-motive force across the membrane. In the mitochondrial-like A-type HCuOs, binding of heavy metal ions at the surface of the protein inhibits proton transfer. In bacterial C-type oxidases, the entry point to the proton pathway is on an accessory subunit unrelated to any subunit in A-type HCuOs. Despite this, we show here that heavy metal ions such as Zn2+ inhibit O-2-reduction very similarly in C-type as in A-type HCuOs, and furthermore that the binding site shares the same Glu-His motif.

• 出版日期2013-3-18