http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Synchrotron-radiation-based <SUP>174</SUP>Yb Mossbauer Spectroscopy of the 1/1 Au-Al-Yb Approximant
Yumi Kinoshita,Hisao Kobayashi,Nobumoto Nagasawa,Yoshitaka Yoda,Ryo Masuda,Yuki Nakamura,Yuya Sakakibara,Kazuhiko Deguchi 한국물리학회 2023 새물리 Vol.73 No.12
The Yb-based valence-uctuating Au-Al-Yb quasicrystal exhibits unconventional quantum critical phenomena with unusual critical indices at low temperatures at ambient pressure. Furthermore, the quantum criticality of the Au-Al-Yb quasicrystal remains robust even under hydrostatic pressure. In contrast, the Au-Al-Yb 1/1 approximant does not display quantum criticality at ambient pressure and quantum criticality appears at approximately 2.0 GPa with the same critical indices as the quasicrystal. In this study, we conducted synchrotron-radiation (SR) -based <SUP>174</SUP>Yb Mossbauer spectroscopy on both the quasicrystal and 1/1 approximant, allowing us to observe di_erences in the 4f electronic states of Yb ions between the quasicrystal and 1/1 approximant.
Nuclear Resonance Vibrational Spectroscopic Definition of Peroxy Intermediates in Nonheme Iron Sites
Sutherlin, Kyle D.,Liu, Lei V.,Lee, Yong-Min,Kwak, Yeonju,Yoda, Yoshitaka,Saito, Makina,Kurokuzu, Masayuki,Kobayashi, Yasuhiro,Seto, Makoto,Que, Lawrence,Nam, Wonwoo,Solomon, Edward I. American Chemical Society 2016 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.138 No.43
<P>Fe-III-(hydro)peroxy intermediates have been isolated in two classes of mononuclear nonheme Fe enzymes that are important in bioremediation: the Rieske dioxygenases and the extradiol dioxygenases. The binding mode and protonation state of the peroxide moieties in-these intermediates are not well-defined, due to a lack of vibrational structural data. Nuclear resonance vibrational spectroscopy (NRVS) is an important technique for obtaining vibrational information on these and other intermediates, as it is sensitive to all normal modes with Fe displacement. Here, we present the NRVS spectra of side-on Fe-III-peroxy and end-on Fe-III-hydroperoxy model complexes and assign these spectra using calibrated DFT calculations. We then use DFT calculations to define and understand the changes in the NRVS spectra that arise from protonation and from opening the Fe-O-O angle. This study identifies four spectroscopic handles that will enable definition of the binding mode and protonation state of Fe-III-peroxy intermediates in mononuclear nonheme Fe enzymes. These structural differences are important in determining the frontier molecular orbitals available for reactivity.</P>