Complex III Subunit 5 Antibody (YA1865),MedChemexpress,HY-P82120

Complex III Subunit 5 is a component of the ubiquinol-cytochrome c oxidoreductase (also known as cytochrome b-c1 complex or complex III, CIII), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain, driving oxidative phosphorylation. The respiratory chain comprises three multisubunit complexes: succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (complex III, CIII), and cytochrome c oxidase (complex IV, CIV), which cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, generating an electrochemical gradient across the inner membrane that powers transmembrane transport and ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, coupling this redox reaction to proton translocation across the mitochondrial inner membrane, with protons carried as hydrogens on the quinol. In the Q cycle, two protons are consumed from the matrix, four protons are released into the intermembrane space, and two electrons are transferred to cytochrome c. The Rieske protein, a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster, cycles between two conformational states during catalysis to transfer electrons from the quinol bound at the Q(0) site in cytochrome b to cytochrome c1 (by similar). Incorporation of UQCRFS1 is the penultimate step in complex III assembly. UQCRFS1 undergoes proteolytic processing after integration into the complex III dimer, with one fragment, subunit 9, corresponding to its mitochondrial targeting sequence (MTS). This processing is essential for proper insertion of UQCRFS1 into the complex III dimer, but persistent UQCRFS1-derived fragments may hinder the processing and assembly of newly imported UQCRFS1 into complex III, adversely affecting its structure and function.

petC; PGR1; RIP1; RIS1; RISP; UQCR5; UQCRFS1