Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity Analysis of Cytochrome <i>c</i>

Johannessen, Christian; White, P.C.; Abdali, Salim

doi:10.1021/jp0705267

Cited by 71 publications

(95 citation statements)

References 26 publications

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“…Synthetic surfactant-free P99/30nm NanoSun ZnO nanoparticles (ZnONPs, purity 99.5%, specific surface area: 38 m 2 /g, density: 5,52 ±0.05 g/cm 3 , zeta potential in DI water: 20.7 ±2.0 mV (Heggelund et al 2013)) were obtained from Microniser Pty Ltd (Dandenong, Australia). NanoSun P99/30 ZnO, which is manufactured by milling, has no coatings or surface modifications and is close to spherical in shape.…”

Section: Preparation Of Znonpsmentioning

confidence: 99%

Metalloproteins and phytochelatin synthase may confer protection against zinc oxide nanoparticle induced toxicity in Caenorhabditis elegans

Polak

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Jurkschat

et al. 2014

Comparative Biochemistry and Physiology Part C: Toxicology &

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Spurgeon, David J.; Sturzenbaum, Stephen R.. 2014. Metalloproteins and phytochelatin synthase may confer protection against zinc oxide nanoparticle induced toxicity in Caenorhabditis elegansContact CEH NORA team at noraceh@ceh.ac.ukThe NERC and CEH trademarks and logos ('the Trademarks') are registered trademarks of NERC in the UK and other countries, and may not be used without the prior written consent of the Trademark owner. suggesting that the nominal exposure to pure ZnONPs represents in vivo, at best, a mixture exposure of ionic zinc and nanoparticles. Nevertheless, the analyzes provided evidence that the metallothioneins (mtl-1 and mtl-2), the pytochelatin synthase (pcs-1) and an apoptotic marker (cep-1) were transcriptionally activated. In addition, the DCFH-DA assay provided in vitro evidence of the oxidative potential of ZnONPs in the metal exposure sensitive triple mutant.Raman spectroscopy highlighted that the biomolecular phenotype changes significantly in the metal sensitive knockout worm upon ZnONP exposure, suggesting that these metalloproteins are instrumental in the protection against cytotoxic damage. Finally, ZnONP exposure was shown to decrease growth and development, reproductive capacity and lifespan, effects which were amplified in the triple knockout. By combining diverse toxicological strategies, we identified that individuals (genotypes) housing mutations in key metalloproteins are more susceptible to ZnONP exposure, which underlines the importance of fully functional metalloproteins to minimize ZnONP induced toxicity.

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Section: Preparation Of Znonpsmentioning

confidence: 99%

Metalloproteins and phytochelatin synthase may confer protection against zinc oxide nanoparticle induced toxicity in Caenorhabditis elegans

Polak

Read

Jurkschat

et al. 2014

Comparative Biochemistry and Physiology Part C: Toxicology &

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“…Assignments of the peaks in the RRS spectrum of Hb and their attributions to vibration of certain heme bonds and the sensitivity to ligands were done according to earlier studies. 21,[35][36][37] Analysis of RRS and SERRS spectra of the Hb shows that most of the peaks have the same positions, which indicates the absence of artifact peak shifts caused by Ag NPs. The reference spectrum of a mixture of Ag NP colloids and water only can also be seen in Figure 1b (grey), which shows clearly that the SERRS peaks are attributed to the Hb in the sample.…”

Section: Resultsmentioning

confidence: 95%

“…For instance, there are more details in the SERRS spectrum and they appear with higher intensities, e.g. in the frequency region between 1200-600 cm 21 , than in the RRS spectrum. The dominant peaks in SERRS spectrum are those at 1375 cm 21 (symmetric pyrrol half-ring vibrations, m 4 ) and at 1172 cm 21 (asymmetric pyrrol half-ring vibrations, m 30 ), whereas in the RRS spectrum the dominant peaks appear at 1640 cm 21 (C a C m , C a C m H, C a C b bond vibrations, m 10 ) and at 1588 cm 21 (C a C m , C a C m H bond vibrations, m 37 ) appear with the highest intensities.…”

Section: Resultsmentioning

confidence: 99%

“…The optimization showed that there was a strong interplay correlated to the concentration of each component in the measured sample, and by first obtaining the best SERS signal, SEROA was achieved. Additionally, the optimization process was later repeated on cytochrome c (cyt-c), 21 and the optimized conditions of SERS successfully provided another SEROA spectrum, adding to that of enkephalin and myoglobin.…”

Section: Introductionmentioning

confidence: 99%

“…We report here on the employment of an optimization method, by which it was for the first time possible to obtain SERROA (and SERRS) spectra of Hb, thus, it could be considered as another novel SERROA observation of a metalloprotein, besides the earlier SERROA studies of Mb 20 and cyt-c. 21 …”

Section: Introductionmentioning

confidence: 99%

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Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy

Brazhe

Sosnovtseva

et al. 2009

Chirality

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The metalloprotein hemoglobin (Hb) was studied using surface enhanced resonance Raman spectroscopy (SERRS) and surface enhanced resonance Raman optical activity (SERROA). The SERROA results are analyzed and compared with the SERRS, and the later to the resonance Raman (RRS) performed on Hb. The SERRS measurements careful optimization, with respect to the concentration and volume ratio of the analyte to colloids, enables for the first time SERROA of this molecule. We observed that the most intense SERROA signals were attributed the m 4 , m 20 , and m 21 vibrations, which are sensitive to the redox state of the heme's iron ion, and to the presence of its sixth site, bound to exogenous ligand; O 2 , NO or CO. However, in this study, the SERROA signals corresponding to these vibrations appear more sensitive to the Hb oxygen-binding properties than they appear in the SERRS or RRS. Moreover, the SER-ROA signal of Hb has successfully been monitored as a function of time, and was observed to be stable for 4-5 min. To our knowledge, the SERROA results of Hb, and its comparison to SERRS and RRS, are here reported for the first time.

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Chiral R aman and Single Molecule Spectroscopy

Abdali

Blanch

2009

Digital Encyclopedia of Applied Physics

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Chiral Raman spectroscopy, widely known as Raman optical activity (ROA) , is a vibrational tool, which besides information on structure and folding of molecules, provides information on their chirality. This tool has been employed since the early 1970 s; however, it has been limited to very few groups within the vibrational spectroscopy community, because using this tool several requirements for the instrumentation as well as the sample condition and detection have to be fulfilled. Although the first requirement concerns full control of the polarization state of the light, simultaneously for the right‐ and left‐circular polarization states, the latter requirement concerns high concentration of the sample. Consequently and because of the signal collection involving subtraction of the left‐ and right scattered light, the ROA signal is much weaker than the Raman, thus requires much longer acquisition times. After the discovery of the surface‐enhanced Raman scattering (SERS) effect in 1974, the hope of combining SERS with ROA (into surface‐enhanced Raman optical activity (SEROA)) grew high, in that the giant signal provided by SERS was thought to enable much faster ROA measurements and for much lower concentration, even down to the single molecule level. Nevertheless, three decades passed before SEROA studies began to appear in the literature. In spite of the fact that these studies are not yet at the single molecule level, they do provide SEROA from very low concentration (below μM). Here, we introduce SEROA's historical background, theory, instrumentation, and the recent results, achieved by the authors' research groups.

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Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity Analysis of Cytochrome c

Cited by 71 publications

References 26 publications

Metalloproteins and phytochelatin synthase may confer protection against zinc oxide nanoparticle induced toxicity in Caenorhabditis elegans

Metalloproteins and phytochelatin synthase may confer protection against zinc oxide nanoparticle induced toxicity in Caenorhabditis elegans

Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy

Chiral R aman and Single Molecule Spectroscopy

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