Overview of mitochondrial cuproenzymes and copper chaperones. (A) Electron transport chain (complexes I–IV and ATP synthase) in the inner membrane of mitochondria. The complex IV renowned as cytochrome c oxidase (CcO) can reduce O2 into H2O, pumping proton from the matrix to the intermembrane space (IMS) to establish an electrochemical gradient for ATP synthesis. Mitochondrial SOD1 could detoxify superoxide anion (O2•−). Metallochaperones including Cox17, Sco1/2, Cox17, Cox11, and CCS mediate copper insertion into the cuproenzymes. (B) Coordination sphere of CuA site, heme a, and heme a3/CuB in CcO (PDB 5Z62). (C) Coordination sphere of Cox11 (PDB 1SO9).
Regulation of CMGC kinases by prolyl hydroxylation. The activation of DYRK1s, a group of CMGC kinases, critically relies on the autophosphorylation of a tyrosine residue within the activation loop of the catalytic domain. This essential autophosphorylation event takes place during the kinase’s folding process and is facilitated by a unique folding intermediate. Notably, this folding intermediate differs from the mature conformation that results from prolyl hydroxylation by PHDs.
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