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Sökning: WFRF:(Onoue Y)

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1.
  • 2017
  • swepub:Mat__t
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2.
  • Noboriguchi, Akatoki, et al. (författare)
  • Extreme Nature of Four Blue-excess Dust-obscured Galaxies Revealed by Optical Spectroscopy
  • 2022
  • Ingår i: Astrophysical Journal. - : American Astronomical Society. - 1538-4357 .- 0004-637X. ; 941:2
  • Tidskriftsartikel (refereegranskat)abstract
    • We report optical spectroscopic observations of four blue-excess dust-obscured galaxies (BluDOGs) identified by the Subaru Hyper Suprime-Cam. BluDOGs are a subclass of dust-obscured galaxies (DOGs; defined with the extremely red color (i − [22])AB ≥ 7.0; Toba et al., showing a significant flux excess in the optical g and r bands over the power-law fits to the fluxes at the longer wavelengths. Noboriguchi et al. have suggested that BluDOGs may correspond to the blowing-out phase involved in a gas-rich major-merger scenario. However, the detailed properties of BluDOGs are not understood because of the lack of spectroscopic information. In this work, we carry out deep optical spectroscopic observations of four BluDOGs using Subaru/FOCAS and VLT/FORS2. The obtained spectra show broad emission lines with extremely large equivalent widths, and a blue wing in the C iv line profile. The redshifts are between 2.2 and 3.3. The averaged rest-frame equivalent widths of the C iv lines are 160 ± 33 Å, ∼7 times higher than the average of a typical type 1 quasar. The FWHMs of their velocity profiles are between 1990 and 4470 km s−1, and their asymmetric parameters are 0.05 and 0.25. Such strong C iv lines significantly affect the broadband magnitudes, which are partly the origin of the blue excess seen in the spectral energy distribution of BluDOGs. Their estimated supermassive black hole masses are 1.1 × 108 < M BH/M ⊙ <5.5 × 108. The inferred Eddington ratios of the BluDOGs are higher than 1 (1.1 < λ Edd < 3.8), suggesting that the BluDOGs are in a rapidly evolving phase of supermassive black holes.
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3.
  • Onoue, Y., et al. (författare)
  • A giant liposome for single-molecule observation of conformational changes in membrane proteins
  • 2009
  • Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 1879-2642 .- 0005-2736. ; 1788:6, s. 1332-1340
  • Tidskriftsartikel (refereegranskat)abstract
    • We present an experimental system that allows visualization of conformational changes in membrane proteins at the single-molecule level. The target membrane protein is reconstituted in a giant liposome for independent control of the aqueous environments on the two sides of the membrane. For direct observation of conformational changes, an extra-liposomal site(s) of the target protein is bound to a glass surface, and a probe that is easily visible under a microscope, such as a micron-sized plastic bead, is attached to another site on the intra-liposomal side. A conformational change, or an angular motion in the tiny protein molecule, would manifest as a visible motion of the probe. The attachment of the protein on the glass surface also immobilizes the liposome, greatly facilitating its manipulation such as the probe injection. As a model system, we reconstituted ATP synthase (FOF1) in liposomes tens of mu m in size, attached the protein specifically to a glass surface, and demonstrated its ATP-driven rotation in the membrane through the motion of a submicron bead. (c) 2009 Elsevier B.V. All rights reserved.
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