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Potential Role of Sulfur-Containing Antioxidant Systems in Highly Oxidative Environments
Open AccessArticle

Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus vannamei

Departamento de Medicina molecular y Bioprocesos, Instituto de Biotecnología (IBT), Universidad Nacional Autónoma de México (UNAM), Avenida Universidad 2001, Colonia Chamilpa, Cuernavaca 62210, Mexico
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Molecules 2014, 19(12), 21113-21126; https://doi.org/10.3390/molecules191221113
Received: 10 October 2014 / Revised: 6 December 2014 / Accepted: 9 December 2014 / Published: 15 December 2014
(This article belongs to the Special Issue Sulfur Atom: Element for Adaptation to an Oxidative Environment)
Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx) revealed a dimeric form of the protein mediated by a covalent link through a disulfide bond between Cys73 from each monomer. In the present study, X-ray-induced damage in the catalytic and the interface disulfide bond of LvTrx was studied at atomic resolution at different transmission energies of 8% and 27%, 12.8 keV at 100 K in the beamline I-24 at Diamond Light Source. We found that at an absorbed dose of 32 MGy, the X-ray induces the cleavage of the disulfide bond of each catalytic site; however, the interface disulfide bond was cleaved at an X-ray adsorbed dose of 85 MGy; despite being the most solvent-exposed disulfide bond in LvTrx (~50 Å2). This result clearly established that the interface disulfide bond is very stable and, therefore, less susceptible to being reduced by X-rays. In fact, these studies open the possibility of the existence in solution of a dimeric LvTrx. View Full-Text
Keywords: disulfide bond; radiation damage; homodimer; thioredoxin 1; Litopenaeus vannamei disulfide bond; radiation damage; homodimer; thioredoxin 1; Litopenaeus vannamei
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Campos-Acevedo, A.A.; Rudiño-Piñera, E. Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus vannamei. Molecules 2014, 19, 21113-21126.

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