Redox-sensitive and metal-dependent cellular proteins

Redox-sensitive and metal-dependent cellular proteins represent a broad and heterogeneous group of molecules that utilize redox-active residues or metal cofactors to regulate their biological activity (Ghezzi et al., 2018). These proteins, which include various enzymes, transcription factors, and signaling molecules, are essential for maintaining cellular homeostasis by responding to changes in the oxidative environment and metal ion availability (Waldron et al., 2009). For instance, redox-sensitive cysteines can undergo reversible modifications that act as molecular switches, while metal ions like zinc, iron, and copper are often required for structural stability or catalytic function (Bush, 2003). Dysregulation of these proteins is a hallmark of several pathological states, including cancer, where altered redox signaling promotes survival, and neurodegenerative diseases, where metal-induced oxidative stress leads to neuronal death (Halliwell & Gutteridge, 2015). Therapeutic interventions targeting this class often involve the use of antioxidants, metal chelators, or small molecules designed to modify specific redox-sensitive sites to restore normal cellular function (Forman et al., 2014). Despite their therapeutic potential, the broad distribution and diverse functions of these proteins present significant challenges for achieving drug selectivity and minimizing off-target effects.

Other names

Redox-regulated proteinsMetalloproteinsMetal-binding proteinsRedox-active proteinsThiol-based redox sensors

Modulation of cellular redox state, chelation of metal ions, or direct modification of redox-sensitive thiol groups to alter protein function and signaling pathways (Forman et al., 2014; Ghezzi et al., 2018).