Santos Velázquez, Lysmarie

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    Insights into sulfhemoglobin detection: Analyzing the correlation of absorption and emission wavelengths
    (2024-05-10) Santos Velázquez, Lysmarie; López Garriga, Juan; College of Arts and Sciences - Sciences; Hernández Rivera , Samuel P.; Castro Rosario, Miguel; Román Velázquez, Félix R.; Department of Chemistry; Malavez Acevedo , Yadira
    The mechanisms underlying the formation of sulfhemoglobin caused by the use of particular drugs and certain sulfur compounds remain unclear. However, the presence of enzymes in mammalian tissues and organs that produce hydrogen sulfide suggests that the process of sulfhemoglobin and sulfmyoglobin formation is more complex than previously thought. This process involves the interaction of hydrogen sulfide with hemoglobin or myoglobin in the presence of oxygen or hydrogen peroxide to generate of sulfhemoglobin or sulfmyoglobin, respectively. Structurally, the chromophore resulting from sulfheme formation is the product of a covalent modification of the heme group. This modification involves the incorporation of a sulfur atom between carbon atoms, forming a sulfur-carbon ring structure across the β-β double bond of the heme pyrrole B, which shows a characteristic optical band around 623 nm and 618 nm for sulfhemoglobin and sulfmyoglobin, respectively. The presence of sulfhemoglobin at concentrations above the physiological range leads to a condition known as sulfhemoglobinemia because it causes cyanosis due to oxygen deficiency. Realizing a diagnosis of this disease has proven to be a significant challenge for the clinical community. This research aimed to develop a fast and accurate method for detecting sulfhemoglobin in blood samples to improve sulfhemoglobin detection. To achieve this objective, various reactions between oxyhemoglobin and hydrogen sulfide at physiological pH were evaluated using UV-vis and fluorescence spectroscopic techniques. The results demonstrated a direct correlation between the electronic charge transfer transition of sulfhemoglobin at 623 nm and the emission wavelength of 460 nm when excited in the Soret band at 420 nm, which is not observed for oxyhemoglobin or methemoglobin. This novel approach allows for the measurement of sulfhemoglobin levels in a range from 0.02% to 13.5% in mixtures of methemoglobin and oxyhemoglobin. Although further studies are still required, these results indicate that the simultaneous evaluation of the electronic transition of sulfhemoglobin at 623 nm and the emission wavelength at 460 nm when excited in the Soret band at 420 nm is a valuable technique for identifying and quantifying sulfhemoglobin levels in the blood, thus facilitating its diagnosis.