Marchany Rivera, Darya

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    Crystal structures of hemeproteins: Sulf and H2S myoglobin derivatives and Lucina pectinata Oxy (HbII-HbIII) and Oxy (HbIII-HbIII) systems
    (2020-04-21) Marchany Rivera, Darya; López Garriga, Juan; College of Arts and Sciences - Sciences; López Moreno, Martha L.; Rios Steiner, Jorge; Hernandez Rivera, Samuel P.; Santana, Alberto; Department of Chemistry; Velázquez Figueroa, Carlos
    As a gasotransmitter, hydrogen sulfide (H2S) biochemistry in humans is of pivotal importance. One relevant reaction of H2S in our bodies is its interaction with hemeproteins. The threshold of its beneficial/harmful effects relies on concentration. Nevertheless, in other kingdoms of life, evolution has adapted some of these hemeproteins to be functional under H2S levels, with different functions than in humans. Regarding this, to have an insight into the hemeprotein’s interactions and H2S, the formation of myoglobin sulfheme derivatives was explored by UV-vis, in the presence of hydrogen sulfide, dimethyl sulfide, and sodium thiomethoxide. The results show that the H-S group is essential for the presence of the 620 nm band attributed to SulfMb. Also, the cyano-sulfmyoglobin (SMb-CN) complex was used to define sulfheme isomers upon the reaction of Mb with H2O2 in the presence of H2S. The results show that the crystallization of the SMb-CN derivative is extremely temperature-dependent in order to achieve high purity and stability. The interactions of Mb crystals with H2S was pursued. Results show the viability to determine reaction times and the possibility of trapping plausible reaction intermediates. Simultaneously, the oxygen carriers HbII and HbIII from Lucina pectinata were resolved as the complex oxy (HbII-HbIII) at pH 5, 6, and 7 by X-ray crystallography and oxy-(HbIII-HbIII) by SAXS structures. The former results suggests that the stability of oxy-(HbII-HbIII) heterodimer towards met-(HbII-HbIII) is a function of pH, and it could be the driving force for oxygen release in the clam symbionts. The latter results confirmed the existence of the oxy (HbIII-HbIII) homodimer, not previously reported, as another probable structure capable of supplying O2 to L. pectinata’s bacterial system.