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<p>and Tyr83 of subunit D. The quinone ring is surrounded by Ile28 of subunit C and Pro160 of subunit B. These <a href="page.php?w=Residue_%28chemistry%29">residues</a>, along with Il209, Trp163, and Trp164 of subunit B, and Ser27 (C atom) of subunit C, form the <a href="page.php?w=hydrophobic">hydrophobic</a> environment of the <a href="page.php?w=quinone">quinone</a>-binding pocket Qp. In contrast, ubiquinone binding site Q<sub>D</sub>, which lies closer to inter-membrane space, is composed of SDHD only and has lower affinity to ubiquinone.</p>

<p><big> Succinate binding site </big></p><p>
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