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- Ho, Anna Y. Q., et al.
(författare)
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Cosmological Fast Optical Transients with the Zwicky Transient Facility : A Search for Dirty Fireballs
- 2022
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Ingår i: Astrophysical Journal. - : American Astronomical Society. - 0004-637X .- 1538-4357. ; 938:1
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Tidskriftsartikel (refereegranskat)abstract
- Dirty fireballs are a hypothesized class of relativistic massive-star explosions with an initial Lorentz factor Γinit below the Γinit ∼ 100 required to produce a long-duration gamma-ray burst (LGRB), but which could still produce optical emission resembling LGRB afterglows. Here we present the results of a search for on-axis optical afterglows using the Zwicky Transient Facility (ZTF). Our search yielded seven optical transients that resemble on-axis LGRB afterglows in terms of their red colors (g − r > 0 mag), faint host galaxies (r > 23 mag), rapid fading (dr/dt > 1 mag day−1), and in some cases X-ray and radio emission. Spectroscopy of the transient emission within a few days of discovery established cosmological distances (redshift z = 0.876 to 2.9) for six of the seven events, tripling the number of afterglows with redshift measurements discovered by optical surveys without a γ-ray trigger. A likely associated LGRB (GRB 200524A, GRB 210204A, GRB 210212B, and GRB 210610B) was identified for four events (ZTF 20abbiixp/AT 2020kym, ZTF 21aagwbjr/AT 2021buv, ZTF 21aakruew/AT 2021cwd, and ZTF 21abfmpwn/AT 2021qbd) post facto, while three (ZTF 20aajnksq/AT 2020blt, ZTF 21aaeyldq/AT 2021any, and ZTF 21aayokph/AT 2021lfa) had no detected LGRB counterpart. The simplest explanation for the three "orphan" events is that they were regular LGRBs missed by high-energy satellites owing to detector sensitivity and duty cycle, although it is possible that they were intrinsically subluminous in γ-rays or viewed slightly off-axis. We rule out a scenario in which dirty fireballs have a similar energy per solid angle to LGRBs and are an order of magnitude more common. In addition, we set the first direct constraint on the ratio of the opening angles of the material producing γ-rays and the material producing early optical afterglow emission, finding that they must be comparable.
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| 2. |
- Zhang, Rong guang, et al.
(författare)
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Structure of Escherichia coli ribose-5-phosphate isomerase : a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle
- 2003
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Ingår i: Structure. - 0969-2126 .- 1878-4186. ; 11:1, s. 31-42
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Tidskriftsartikel (refereegranskat)abstract
- Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for acid-base catalysis is proposed.
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| 3. |
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| 4. |
- Zhang, Rong-Guang, et al.
(författare)
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The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction
- 2003
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Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 332:5
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Tidskriftsartikel (refereegranskat)abstract
- Ribose-5-phosphate isomerases (EC 5.3.1.6) interconvert ribose 5-phosphate and ribulose 5-phosphate. This reaction permits the synthesis of ribose from other sugars, as well as the recycling of sugars from nucleotide breakdown. Two unrelated types of enzyme can catalyze the reaction. The most common, RpiA, is present in almost all organisms (including Escherichia coli), and is highly conserved. The second type, RpiB, is present in some bacterial and eukaryotic species and is well conserved. In E.coli, RpiB is sometimes referred to as AlsB, because it can take part in the metabolism of the rare sugar, allose, as well as the much more common ribose sugars. We report here the structure of RpiB/AlsB from E.coli, solved by multi-wavelength anomalous diffraction (MAD) phasing, and refined to 2.2A resolution. RpiB is the first structure to be solved from pfam02502 (the RpiB/LacAB family). It exhibits a Rossmann-type alphabetaalpha-sandwich fold that is common to many nucleotide-binding proteins, as well as other proteins with different functions. This structure is quite distinct from that of the previously solved RpiA; although both are, to some extent, based on the Rossmann fold, their tertiary and quaternary structures are very different. The four molecules in the RpiB asymmetric unit represent a dimer of dimers. Active-site residues were identified at the interface between the subunits, such that each active site has contributions from both subunits. Kinetic studies indicate that RpiB is nearly as efficient as RpiA, despite its completely different catalytic machinery. The sequence and structural results further suggest that the two homologous components of LacAB (galactose-6-phosphate isomerase) will compose a bi-functional enzyme; the second activity is unknown.
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