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rHbI‐S 2 H as a Potential Novel Hydrogen Sulfide Donor
Author(s) -
Oliveras Alfredo Reyes,
Arias Hazel Borges,
LópezGarriga Juan
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb25
Subject(s) - chemistry , heme , antioxidant , hemoglobin , hydrogen sulfide , myoglobin , biochemistry , pharmacology , enzyme , medicine , sulfur , organic chemistry
Hydrogen sulfide (H 2 S) is a well‐known poisonous gas whose toxic effects have been studied for many years. In recent studies, it was found that H 2 S is produced endogenously in humans through enzymatic pathways and has functioned as a vasodilator, anti‐inflammatory, an antioxidant and smooth muscle relaxant. As result, current studies of H 2 S are focused as a signaling molecule involved in various physiological processes like NO and CO. Also, H 2 S concentration in human physiology has been associated with diseases like hypertension, Alzheimer's, cancer, arthritis, diabetes, ulcerative colitis and cardiovascular diseases. Biochemical and physiological studies of H 2 S have been performed by using compounds that release or promote the production of H 2 S in biological samples for its therapeutic attribution known as H 2 S donors. Hemoglobin I (HbI) is a hemoprotein found in the clam Lucina pectinata that has the property of binding H 2 S in its heme group forming the HbI‐SH 2 complex. For this reason, the viability of the HbI from L. pectinata was studied for the delivery of H 2 S in biological systems to obtain a reliable H‐ 2 S donor. Kinetics studies were performed using a UVV is spectroscopy at physiological conditions with the following parameters; Krebs' buffer at pH 7.4 and 25°C and 37 °C for 24 hours. During the 24 hours, the Soret band showed a displacement from 426 nm (HbI‐SH 2 ) to 407 nm (HbI met ) indicating the release of H 2 S from the protein. The half‐life of the complex was approximately 6 hours. The dissociation constant (k off ) 0.43×10 −3 seg −1 . This result shows the high affinity of the H 2 S for the protein regardless of physiological pH and buffer. Support or Funding Information This work was funded by the National Science Foundation STC award number 1231306. Research reported in this publication was supported by the National Institute Of General Medical Sciences of the National Institutes of Health under Award Number T34GM008419. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .