RESUMO
Vibrational Fourier-transform infrared (FTIR) spectroscopy aided with molecular dynamics (MD) simulations is used for studying the interaction of several reactive aldehydes (RAs), nonanal (NA), 2-nonenal (NE), 4-hydroxy-2-nonenal (HNE) and 4-oxo-2-nonenal (ONE), with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) bilayer. The results obtained by the combination of these two techniques, supported also by electron paramagnetic resonance (EPR) spectroscopy, show that NA has the strongest stabilization in the bilayer, followed by less stabilized NE, HNE and ONE. We also revealed that HNE readily makes hydrogen bonds to carbonyl groups of POPC (but not to phosphate groups), in contrast to other RAs which are hydrogen bond acceptors and do not make hydrogen bonds with lipids. A combination of FTIR spectroscopy and MD simulations is sensitive to small chemical changes in the structures of RAs, thus making it a valuable tool for studying the weak interactions between compounds inserted to phospholipid bilayers.
Assuntos
Aldeídos/química , Bicamadas Lipídicas/química , Simulação de Dinâmica Molecular , Fosfolipídeos/química , Espectroscopia de Ressonância de Spin Eletrônica , Estrutura MolecularRESUMO
In this article, we present the novel application of the nuclear spin bath model and the cluster correlation expansion method on studying the matrix material structure via embedded electron spin decoherence. Profiles of embedded electron spin decoherence under the Carr-Purcell-Meiboom-Gill dynamical decoupling pulse series in a model system for organic solids (malonic acid) are calculated for different structures. Resulting decay profiles exhibit a strong correlation to the variations of an adjacent proton environment among them. In addition, the decoherence behavior of embedded spin in proton spin bath(s) of organic solids is found to be significantly different from bath models with other nuclei through the violation of the even-odd pulse parity, which characterizes the influence of large dipolar coupling between protons at the quantum level. Theoretical predictions of decoherence profiles in polycrystalline, the relative distribution of Hahn echo signal decay time scales among single crystal orientations, and the reduction in Hahn echo signal decay time scale by disorder are positively verified by experiments.
RESUMO
In photosynthesis, final electron transfer from ferredoxin to NADP(+) is accomplished by the flavo enzyme ferredoxin:NADP(+) oxidoreductase (FNR). FNR is recruited to thylakoid membranes via integral membrane thylakoid rhodanase-like protein TROL. We address the fate of electrons downstream of photosystem I when TROL is absent. We have employed electron paramagnetic resonance (EPR) spectroscopy to study free radical formation and electron partitioning in TROL-depleted chloroplasts. DMPO was used to detect superoxide anion (O2(.-)) formation, while the generation of other free radicals was monitored by Tiron. Chloroplasts from trol plants pre-acclimated to different light conditions consistently exhibited diminished O2(.-) accumulation. Generation of other radical forms was elevated in trol chloroplasts in all tested conditions, except for the plants pre-acclimated to high-light. Remarkably, dark- and growth light-acclimated trol chloroplasts were resilient to O2(.-) generation induced by methyl-viologen. We propose that the dynamic binding and release of FNR from TROL can control the flow of photosynthetic electrons prior to activation of the pseudo-cyclic electron transfer pathway.
Assuntos
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Transporte de Elétrons , Ferredoxina-NADP Redutase/metabolismo , Proteínas de Membrana/metabolismo , Redes e Vias Metabólicas , Fotossíntese , Cloroplastos/metabolismo , Oxigênio/metabolismo , Fotoperíodo , Espécies Reativas de Oxigênio/metabolismoRESUMO
EPR spectroscopy was used to examine the magnetic properties of two enzymatically synthesized polyaniline (PANI) samples obtained in the presence of submicrometer-sized vesicles formed from sodium bis(2-ethylhexyl)sulfosuccinate (AOT) as templates. PANI-HRPC-AOT was synthesized with horseradish peroxidase isoenzyme C (HRPC) and hydrogen peroxide (H2O2) as oxidant while PANI-TvL-AOT was prepared with Trametes versicolor laccase (TvL) and dioxygen (O2) as oxidant. A commercial conductive sample of the emeraldine salt form of polyaniline (PANI-ES) was also used for comparison in order to correlate the experimental data obtained for PANI-HRPC-AOT and PANI-TvL-AOT with the properties of the well-characterized PANI-ES. It was shown that a model based on the concept of correlated polaronic bands could be applied for the interpretation of the EPR spectra of all three examined samples, although PANI-HRPC-AOT and PANI-TvL-AOT were significantly less conductive than PANI-ES. The magnetic properties of the PANI samples could be related to their conductivities, whereby a low conductivity was ascribed to decreased interchain spin interactions which were detectable from a splitting of the triplet spectrum at low temperatures (5-10 K). The obtained effective distance between the polyaniline chains is larger for enzymatically synthesized PANI than for PANI-ES, most likely mainly due to the presence of AOT which could not be removed completely during the work-up. AOT influences the chain conformation and the average chain-chain distance.
RESUMO
The importance of turn-like peptide conformation for the copper(II) binding has been revealed by the synthesis of simple amino acid-based tweezers and the study of their interaction with copper(II). Amino acids Phe, Leu, Val, Ala and Gly were bridged through their C-terminuses with conformationally constrained motif, cis enediyne moiety ((Z)-octa-4-en-2,6-diyne-1,8-diamine). The interaction of prepared diamine ligands with copper(II) was studied by means of potentiometric titrations, UV-visible and EPR spectroscopic and mass spectrometric techniques. All ligands interact efficiently with copper(II) and form complexes of 1:1 stoichiometry differing in the protonation state of the ligand. LCu(2+) species were found predominant at pH<6.5, with log K* ranging from -8.06 to -6.65, while at higher pH deprotonation occurred, giving rise to LH(-1)Cu(+) complexes or LH(-2)Cu complex for the phenylalanine-related ligand. An additional species, LH(-3)Cu(-) were found at pH>9 for the valine- and alanine-related ligands, respectively. Comparing stability of studied complexes with those reported in previous work revealed that ligands effectively emulate properties of copper(II) binding peptides. Based on the results obtained in this work it can be concluded that structural rigidity significantly enhances coordination properties of the ligand, thus conforming importance of the turn-like peptide conformation for the copper(II) binding.
Assuntos
Aminoácidos/química , Cobre/química , Espectroscopia de Ressonância de Spin Eletrônica , Ligantes , Ligação Proteica , Conformação Proteica , Espectrofotometria UltravioletaRESUMO
The absorption and fluorescence spectra of indole-3-acetic acid (1), a plant growth regulator (auxin) and experimental cancer therapeutic, 29 ring-substituted derivatives and the 7-aza analogue (1H-pyrrolo[2,3b]pyridine-3-acetic acid) are compared. Two to four absorbance maxima in the 260-310-nm range are interpreted as overlapping vibronic lines of the 1La<--1A and 1Lb<--1A transitions. Two further maxima in the 200-230-nm region are assigned to the 1Ba<--1A and 1Bb<--1A transitions. 4- and 7-Fluoroindole-3-acetic acid exhibit blue shifts with respect to 1, most other derivatives show red shifts. All indole-3-acetic acids studied, with the exception of chloro-, bromo- and 4- or 7-fluoro-derivatives, fluoresce at 345-370 nm when excited at 275-280 nm. 7-Azaindole-3-acetic acid emits at 411 nm. The fluorescence quantum yield of 6-fluoroindole-3-acetic acid significantly exceeds that of 1 (0.3); the other derivatives have lower quantum yields. The plant-growth promoting activity of the ring-substituted indole-3-acetic acids studied correlates with the position of the 1Bb<--1A transition band.