hCTR1 has the capacity to reduce Cu(II)

yet another nail to the coffin of MitoSynergy’s foundational ideas (that Cu2+ can’t be used by the body):

Though in vitro studies from Haas group have shown that purified N-terminus of hCTR1 has the capacity to reduce Cu(II) in the presence of ascorbate;

This N-terminal extracellular domain contains multiple methionines (M7GM9, the first Met-cluster and 40MMMMPM45, the second Met cluster) and histidine (H3-H6, H22-H24, and H31-H33) rich clusters that are possible anchoring sites for Cu(I) and Cu(II) ions, respectively. After shuttling through the N-terminus, the reduced copper is then passed through a Cu(I) specific selectivity filter formed by a conserved 150MXXXM154 sequence (R1)

References

1
Copper(II) import and reduction are dependent on His-Met clusters in the extracellular amino terminus of human copper transporter-1
2022