Dent, Matthew R. published the artcileElectron Paramagnetic Resonance Spectroscopy as a Probe of Hydrogen Bonding in Heme-Thiolate Proteins, HPLC of Formula: 119-80-2, the publication is Inorganic Chemistry (2019), 58(23), 16011-16027, database is CAplus and MEDLINE.
Despite utilizing a common cofactor binding motif, hemoproteins bearing a cysteine-derived thiolate ligand (heme-thiolate proteins) are involved in a diverse array of biol. processes ranging from drug metabolism to transcriptional regulation. Though the origin of heme-thiolate functional divergence is not well understood, growing evidence suggests that the hydrogen bonding (H-bonding) environment surrounding the Fe-coordinating thiolate influences protein function. Outside of X-ray crystallog., few methods exist to characterize these critical H-bonding interactions. ESR (EPR) spectra of heme-thiolate proteins bearing a six-coordinate, Fe(III) heme exhibit uniquely narrow low-spin (S = 1/2), rhombic signals, which are sensitive to changes in the heme-thiolate H-bonding environment. To establish a well-defined relationship between the magnitude of g-value dispersion in this unique EPR signal and the strength of the heme-thiolate H-bonding environment, we synthesized and characterized of a series of six-coordinate, aryl-thiolate-ligated Fe(III) porphyrin complexes bearing a tunable intramol. H-bond. Spectroscopic investigation of these complexes revealed a direct correlation between H-bond strength and g-value dispersion in the rhombic EPR signal. Using d. functional theory (DFT), we elucidated the electronic origins of the narrow, rhombic EPR signal in heme-thiolates, which arises from an Fe-S p¦Ð-d¦Ð bonding interaction. Computational anal. of the intramolecularly H-bonded heme-thiolate models revealed that H-bond donation to the coordinating thiolate reduces thiolate donor strength and weakens this Fe-S interaction, giving rise to larger g-value dispersion. By defining the relationship between heme-thiolate electronic structure and rhombic EPR signal, it is possible to compare thiolate donor strengths among heme-thiolate proteins through anal. of low-spin, Fe(III) EPR spectra. Thus, this study establishes EPR spectroscopy as a valuable tool for exploring how second coordination sphere effects influence heme-thiolate protein function. Herein, we utilize exptl. and computational methods to enumerate the electronic origin of the anisotropic rhombic EPR signal characteristic of thiolate-ligated hemoproteins, and we illustrate how EPR spectroscopy may be used to probe the second coordination sphere of heme-bound thiolate. Through synthesis and characterization of porphyrin-thiolate models bearing a tunable, intramol. H-bond, we establish a direct correlation between the magnitude of g-shifts observed in the rhombic EPR signal and thiolate H-bond strength.
Inorganic Chemistry published new progress about 119-80-2. 119-80-2 belongs to catalysis-chemistry, auxiliary class sulfides,Carboxylic acid,Benzene, name is 2,2′-Dithiodibenzoic acid, and the molecular formula is C14H10O4S2, HPLC of Formula: 119-80-2.
Referemce:
https://courses.lumenlearning.com/boundless-chemistry/chapter/catalysis/,
Catalysis – Wikipedia