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Exertional heat stroke (EHS) is a life-threatening condition requiring rapid reversal of hyperthermia to prevent poor health outcomes. Current treatment protocols aim for a cooling rate of 0.15 C/min using various modalities. This case report details a 22-year-old male who, despite initial successful cooling measures, experienced rebound hyperthermia, necessitating the use of endovascular cooling (EVC). The patient collapsed during a 19.3 km (12-mile) ruck march in Fort Moore, Georgia, with an initial core temperature of 41.6ºC. Conventional cooling methods, including ice sheets and chilled intravenous saline, adequately cooled the patient to target temperatures; however, discontinuation of cooling methods resulted in rebound hyperthermia. Endovascular cooling was eventually initiated, resulting in euthermia after 36 hours of continued use. During his hospital admission, the patient was evaluated thoroughly for underlying etiologies contributing to his rebound hyperthermia. This workup did not yield any concerning pathology, except for bilateral foot cellulitis noted on physical examination, which was subsequently managed with antibiotics. Despite initial complications, the patient recovered within 5 days and returned to duty after 2 months. Several case reports have been published regarding the use of EVC in the management of EHS. These reports, however, describe its use in initial management of EHS or in cases where hyperthermia was refractory to other conventional cooling methods. To our knowledge, this is the first report of its kind highlighting its successful implementation in rebound hyperthermia. Early recognition and initiation of cooling measures are critical in EHS cases. Future directions include developing EHS-specific EVC protocols for patients experiencing refractory or rebound hyperthermia., (© The Association of Military Surgeons of the United States 2024. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site–for further information please contact journals.permissions@oup.com.)

Persulfide dioxygenases (PDOs), also known as sulfur dioxygenases (SDOs), oxidize glutathione persulfide (GSSH) to sulfite and GSH. PDOs belong to the metallo-β-lactamase superfamily and play critical roles in animals, plants, and microorganisms, including sulfide detoxification. The structures of two PDOs from human and Arabidopsis thaliana have been reported; however, little is known about the substrate binding and catalytic mechanism. The crystal structures of two bacterial PDOs from Pseudomonas putida and Myxococcus xanthus were determined at 1.5- and 2.5-Å resolution, respectively. The structures of both PDOs were homodimers, and their metal centers and β-lactamase folds were superimposable with those of related enzymes, especially the glyoxalases II. The PDOs share similar Fe(II) coordination and a secondary coordination sphere-based hydrogen bond network that is absent in glyoxalases II, in which the corresponding residues are involved instead in coordinating a second metal ion. The crystal structure of the complex between the Pseudomonas PDO and GSH also reveals the similarity of substrate binding between it and glyoxalases II. Further analysis implicates an identical mode of substrate binding by known PDOs. Thus, the data not only reveal the differences in metal binding and coordination between the dioxygenases and the hydrolytic enzymes in the metallo-β-lactamase superfamily, but also provide detailed information on substrate binding by PDOs., (© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.)