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dc.contributor.advisorLópez-Garriga, Juan
dc.contributor.authorMarchany-Rivera, Darya
dc.date.accessioned2020-10-25T10:41:54Z
dc.date.available2020-10-25T10:41:54Z
dc.date.issued2020-04-21
dc.identifier.urihttps://hdl.handle.net/20.500.11801/2660
dc.description.abstractAs 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.en_US
dc.description.abstractComo gas transmisor, la bioquímica de sulfuro de hidrógeno (H2S) en humanos es de importancia fundamental. Una reacción relevante de H2S en nuestros cuerpos es su interacción con hemoproteínas. El umbral de sus efectos beneficiosos/nocivos se basa en la concentración. Sin embargo, en otros reinos de la vida, la evolución ha adaptado algunas de estas hemoproteínas para ser funcionales bajo niveles de H2S, con funciones diferentes a los humanos. Con respecto a esto, para tener una visión de las interacciones de la hemoproteína y H2S, la formación de derivados de sulfhemo de mioglobina fueron explorados por UV-vis, en presencia de sulfuro de hidrógeno, sulfuro de dimetilo, y tiometóxido de sodio, los resultados muestran que el grupo H-S es esencial para la presencia de la banda en 620 nm atribuidos a SulfMb. Además, el complejo de cianosulfmioglobina (SMb-CN) se utilizó para definir isómeros de sulfhemo tras la reacción de Mb con H2O2 en presencia de H2S. Los resultados muestran que la cristalización del derivado SMb-CN depende extremadamente de la temperatura para lograr una alta pureza y estabilidad. Además, se siguieron las interacciones de cristales de Mb con H2S. Los resultados muestran la viabilidad para determinar tiempos de reacción y la posibilidad de atrapar posibles intermediarios de reacción. Simultáneamente, los portadores de oxígeno HbII y HbIII de Lucina pectinata se resolvieron como el complejo oxi-(HbII-HbIII) a pH 5, 6, y 7 por cristalografía de rayos-X y oxi-(HbIII-HbIII) por estructuras SAXS. El primer resultado sugiere que la estabilidad del heterodímero de oxi-(HbIIHbIII) hacia met-(HbII-HbIII) es una función del pH, y podría ser la fuerza motriz para la liberación de oxígeno en los simbiontes de la almeja. El último resultado confirmó la existencia del homodímero oxi-(HbIII-HbIII), no reportado previamente, como otra estructura probable para suministrar O2 al sistema bacteriano de L. pectinata.en_US
dc.description.sponsorshipThe presented research project was supported by NSF STC Award number 1231306, NIH INBRE Grant 5P20GM103475, the SLOAN MPHD Program fellowship, the SLAC National Accelerator Laboratory, and the Work2Future Foundation. The use of the Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, is supported by the U.S. Department of Energy, Office of Science, and Office of Basic Energy Sciences under Contract No. DE-AC02-76SF00515. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research and by the National Institutes of Health, National Institute of General Medical Sciences (including P41GM103393).en_US
dc.language.isoenen_US
dc.rightsAttribution-NonCommercial 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/us/*
dc.subjectLucina pectinataen_US
dc.subjectHemoproteins - Effect of hydrogen sulfide onen_US
dc.subjectX-ray crystallographyen_US
dc.subjectOxygen deliveryen_US
dc.subject.lcshHemoproteinsen_US
dc.subject.lcshHydrogen sulfideen_US
dc.subject.lcshLucinaen_US
dc.subject.lcshCrystallographyen_US
dc.subject.lcshMyoglobinen_US
dc.titleCrystal structures of hemeproteins: Sulf and H2S myoglobin derivatives and Lucina pectinata Oxy (HbII-HbIII) and Oxy (HbIII-HbIII) systemsen_US
dc.typeDissertationen_US
dc.rights.holder(c) 2020 Darya Marchany Riveraen_US
dc.contributor.committeeLópez-Moreno, Martha L.
dc.contributor.committeeRios Steiner, Jorge
dc.contributor.committeeHernandez Rivera, Samuel P.
dc.contributor.committeeSantana, Alberto
dc.contributor.representativeVelázquez-Figueroa, Carlos
thesis.degree.levelPh.D.en_US
thesis.degree.disciplineApplied Chemistryen_US
dc.contributor.collegeCollege of Arts and Sciences - Sciencesen_US
dc.contributor.departmentDepartment of Chemistryen_US
dc.description.graduationSemesterSpringen_US
dc.description.graduationYear2020en_US


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