Atom Of Histidine Research Articles

Identification of metal binding motifs in protein frameworks to develop novel remediation strategies for Hg2+ and Cr(VI).

Amino acid sequences in metal-binding proteins with chelating properties offer exciting applications in biotechnology and medical research. To enhance their application in bioremediation studies, we explicitly aimed to identify specific metal-binding chelating motifs in protein structures for two significant pollutants, such as mercury (Hg2+) and chromium Cr(V1). For this purpose, we have performed an extensive coordination chemistry approach by retrieving Hg2+ and Cr(V1) binding protein structures from the protein database and validated using the B-factor, a term defining uncertainty of the atoms and with occupancy to obtain the best binding motifs. Our analysis revealed that acidic amino acids like aspartic acid, glutamic acid, and basic amino acids such as cysteine and histidine are predominant in coordinating with these metals. The order of preference in Hg2+-bound structures is predicted to be Cys > His > Asp > Glu, and for Cr(V1) is His > Asp > Glu. Examination of the atomic coordinates and their distance from each metal revealed that the sulfur atoms of cysteine showing more preference towards Hg2+coordination with an atomic distance ranging from 1.5 to 2.9Å. Likewise, oxygen atoms of aspartic acid, glutamic acid and nitrogen atoms of histidine are within 2Å of Cr(V1) coordination. Based on these observations, we obtained C-C-C, C-X(2)-C-C-(X)2-C, H-C-H motifs for Hg2+, and D-X(1)-D, H-X(3)-E motif for Cr(V1) to be shared within the coordination space of 3Å. As a future scope, we propose that the identified metal-binding chelating motifs are oligopeptides and can display on the surface of microorganisms such as Escherichia coli and Saccharomyces cerevisiae for effective removal of natural Hg2+ and Cr(V1) through biosorption. Hence, our results will provide the basis for futuristic bioremediation.

Electronic and Nonlinear Optical Properties of l-Histidine on Silver: A Theoretical and Experimental Approach.

An investigation of the electrostatic interactions between histidine and silver have been analyzed using density functional theory (DFT). Variations in the structural parameters were identified to be significant at those atoms of histidine near the silver cluster. The shifting of frontier molecular orbitals, reduction in bandgap, molecular electrostatic potential (MEP), and overlap of natural bond orbitals (NBO) between silver and histidine have been theoretically calculated. The results confirm the redistribution of charges consequent to the process of adsorption. On the basis of time-dependent density functional theory (TDDFT), two peaks were generated at 301 and 409 nm in the simulated UV-vis spectrum. Theoretical vibrational Raman analysis of the investigated molecules strongly confirms the process of adsorption. Nonlinear optical (NLO) properties are predicted by theoretical studies and confirmed experimentally via open-aperture Z-scan. The adsorption of histidine on silver enhances the NLO parameters, indicating that it is a promising candidate for NLO devices.

Copper ion interaction with the RNase catalytic site fragment of the angiogenin protein: an experimental and theoretical investigation.

The angiogenin protein (Ang) is a member of the vertebrate-specific secreted ribonucleases and one of the most potent angiogenic factors known. Ang is a normal constituent of human plasma and its concentration increases under some physiological and pathological conditions to promote neovascularization. Ang was originally identified as an angiogenic tumour factor, but its biological activity has been found to extend from inducing angiogenesis to promoting cell survival in different neurodegenerative diseases. Ang exhibits weak ribonucleolytic activity, which is critical for its biological functions. The RNase catalytic sites are two histidine residues, His-13 and His-114, and the lysine Lys-40. Copper is also an essential cofactor in angiogenesis and influences angiogenin's biological properties. The main Cu(ii) anchoring site of Ang is His-114, where metal binding inhibits RNase activity of the protein. To reveal the Cu(ii) coordination environment in the C-terminal domain of the Ang protein, we report on the characterization, by means of potentiometric, voltammetric, and spectroscopic (CD, UV-Vis and EPR) methods and DFT calculations, of Cu(ii) complexes formed with a peptide fragment including the Ang sequence 112-117 (PVHLDQ). Potentiometric titrations indicated that [CuLH-2] is the predominant species at physiological pH. EPR, voltammetric data and DFT calculations are consistent with a CuN3O2 coordination mode in which a distorted square pyramidal arrangement of the peptide was observed with the equatorial positions occupied by the nitrogen atoms of the deprotonated amides of the Asp and Leu residues, the δ-N atom of histidine and the oxygen atom of the aspartic carboxylic group. Moreover, two analogous peptides encompassing the PVHLNQ and LVHLDQ sequences were also characterized by using thermodynamic, spectroscopic and DFT studies to reveal the role they play in Cu(ii) complex formation by the carboxylate side chain of the Asp and Pro residues, a known breaking-point in metal coordination.

Valence orbitals and local bond dynamics around N atoms of histidine under X-ray irradiation

The valence orbitals of aqueous histidine under basic, neutral and acidic conditions and their X-ray induced transformations have been monitored through N 1s resonant inelastic X-ray scattering. Using density functional ab initio molecular dynamics simulations in the core-hole state within the Z + 1 approximation, core-excitation-induced molecular transformations are quantified. Spectroscopic evidence for a highly directional X-ray-induced local N-H dissociation within the scattering duration is presented for acidic histidine. Our report demonstrates a protonation-state and chemical-environment dependent propensity for a molecular dissociation, which is induced by the absorption of high energy photons. This case study indicates that structural deformations in biomolecules under exposure to ionizing radiation, yielding possible alteration or loss of function, is highly dependent on the physiological state of the molecule upon irradiation.

ChemInform Abstract: Conformational Regulation of Amyloid β‐Peptide by Lipid Membranes and Metal Ions

AbstractReview: 28 refs.

脂質膜と金属イオンによるアミロイドβペプチドのコンホメーション制御

Conformational transition of monomeric amyloid beta-peptide (Abeta) to a self-associated beta-sheet structure is considered to be an initial step in the development of Alzheimer's disease. Several lines of evidence suggest that physiologically abundant lipid membranes and metal ions are involved in this step. We have demonstrated that Abeta binds to the phosphatidylcholine membrane in the lamellar gel phase but not in the liquid crystalline phase by using fluorescence and circular dichroism spectroscopy. The membrane-bound Abeta molecule takes alpha-helical or beta-sheet structure depending on the temperature. Tightly packed phosphatidylcholine membranes appear to serve as a platform for non-electrostatic binding and self-association of Abeta. We have also examined Zn(II) and Cu(II) binding modes of Abeta by Raman spectroscopy. The Raman spectra demonstrate that three histidine residues in the N-terminal region of Abeta provide primary metal binding sites. Zn(II) binds to the N(tau) atom of histidine and the peptide aggregates through intermolecular His-Zn-His bridges. In contrast, Cu(II) ion is chelated by the N(pi) atom of histidine and deprotonated main-chain amide nitrogens to form a soluble complex. Our findings on the conformational regulation of Abeta may help in better understanding the molecular basis for the development of Alzheimer's disease.