Fig. 2 (IMAGE) Osaka University Caption Model of QhpC/QhpD/QhpG ternary complex. In this complex, QhpC is triply crosslinked at the active-site pocket of QhpD, along with [4Fe<sub>4</sub>S] clusters. Subsequently, a specific Trp residue of the crosslinked QhpC becomes dihydroxylated at the active site of QhpG close to the FAD. The complex formation thus enables efficient and sequential posttranslational modifications. Credit Osaka University Usage Restrictions None License Licensed content Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.