Discovery of an optical counterpart to the hyperluminous X-ray source in ESO 243-49

The existence of black holes of masses ~ 10^2-10^5 Msun has important implications for the formation and evolution of star clusters and supermassive black holes. One of the strongest candidates to date is the hyperluminous X-ray source HLX1, possibly located in the S0-a galaxy ESO243-49, but the lack of an identifiable optical counterpart had hampered its interpretation. Using the Magellan telescope, we have discovered an unresolved optical source with R = (23.80 +/- 0.25) mag and V = (24.5 +/- 0.3) mag within HLX1's positional error circle. This implies an average X-ray/optical flux ratio ~ 500. Taking the same distance as ESO243-49, we obtain an intrinsic brightness M_R = (-11.0 +/- 0.3) mag, comparable to that of a massive globular cluster. Alternatively, the optical source is consistent with a main-sequence M star in the Galactic halo (for example an M4.4 star at ~ 2.5 kpc). We also examined the properties of ESO243-49 by combining Swift/UVOT observations with stellar population modelling. We found that the overall emission is dominated by a ~5 Gyr old stellar population, but the UV emission at ~2000 Ang is mostly due to ongoing star-formation at a rate of ~ 0.03 Msun/yr. The UV emission is more intense (at least a 9-sigma enhancement above the mean) North East of the nucleus, in the same quadrant as HLX1. With the combined optical and X-ray measurements, we put constraints on the nature of HLX1. We rule out a foreground star and a background AGN. Two alternative scenarios are still viable. HLX1 could be an accreting intermediate-mass black hole in a star cluster, which may itself be the stripped nucleus of a dwarf galaxy that passed through ESO243-49, an event which might have caused the current episode of star formation. Or, it could be a neutron star in the Galactic halo, accreting from an M4-M5 donor star.Comment: 7 pages, accepted by MNRAS. Several improvements from Oct 7 version: stronger evidence of the optical counterpart; more accurate estimate of its brightness (a factor of 2 brighter than previously estimated); use of a larger set of Swift/UVOT data to measure the recent star formation rate in ESO243-49; improved discussion and comparison of the competing scenario

Mo\u3csup\u3eV\u3c/sup\u3e Electron Paramagnetic Resonance of Sulfite Oxidase Revisited: The Low-pH Chloride Signal

Valuable information on the active sites of molybdenum enzymes has been provided by MoV electron paramagnetic resonance (EPR) spectroscopy. In recent years, multiple resonance techniques have been extensively used to examine details of the active-site structure, but basic continuous-wave (CW) EPR has not been re-evaluated in several decades. Here, we present a re-examination of the CW EPR spectroscopy of the sulfite oxidase low-pH chloride species and provide evidence for direct coordination of molybdenum by chloride

The characterization and role of zinc binding in yeast Cox4.

Yeast Cox4 is a zinc binding subunit of cytochrome c oxidase. Cox4 is the only cofactor-containing subunit that is not directly part of the catalytic core of the enzyme located in the mitochondrial inner membrane. The Zn(II) site is shown to be distinct from the bovine ortholog, as it results from the x-ray structure of the entire cytochrome c oxidase in having a single histidyl residue and three conserved cysteines residues in the coordination sphere. Substitutions at the Cys ligand positions result in non-functional Cox4 proteins that fail to lead to cytochrome oxidase assembly. Limited function exists in His-119 mutants when overexpressed. Zn(II) binding in Cox4 is, therefore, important for the stability of the complex. The solution structure of yeast Cox4 elucidated by multidimensional NMR reveals a C-terminal globular domain consisting of two beta sheets analogous to the bovine ortholog except the loop containing the coordinating His in the yeast protein and the fourth Cys in the bovine protein are in different positions in the two structures. The conformation of this loop is dictated by the different sequence position of the fourth coordinating zinc ligand. The Zn(II) ion is buried within the domain, consistent with its role in structural stability. Potential functions of this matrix-facing subunit are discussed

Copper sensing function of Drosophila metal-responsive transcription factor-1 is mediated by a tetranuclear Cu(I) cluster

Drosophila melanogaster MTF-1 (dMTF-1) is a copper-responsive transcriptional activator that mediates resistance to Cu, as well as Zn and Cd. Here, we characterize a novel cysteine-rich domain which is crucial for sensing excess intracellular copper by dMTF-1. Transgenic flies expressing mutant dMTF-1 containing alanine substitutions of two, four or six cysteine residues within the sequence 547CNCTNCKCDQTKSCHGGDC565 are significantly or completely impaired in their ability to protect flies from copper toxicity and fail to up-regulate MtnA (metallothionein) expression in response to excess Cu. In contrast, these flies exhibit wild-type survival in response to copper deprivation thus revealing that the cysteine cluster domain is required only for sensing Cu load by dMTF-1. Parallel studies show that the isolated cysteine cluster domain is required to protect a copper-sensitive S. cerevisiae ace1Δ strain from copper toxicity. Cu(I) ligation by a Cys-rich domain peptide fragment drives the cooperative assembly of a polydentate [Cu4-S6] cage structure, characterized by a core of trigonally S3 coordinated Cu(I) ions bound by bridging thiolate ligands. While reminiscent of Cu4-L6 (L = ligand) tetranuclear clusters in copper regulatory transcription factors of yeast, the absence of significant sequence homology is consistent with convergent evolution of a sensing strategy particularly well suited for Cu(I

Copper sensing function of Drosophila metal-responsive transcription factor-1 is mediated by a tetranuclear Cu(I) cluster

Drosophila melanogaster MTF-1 (dMTF-1) is a copper-responsive transcriptional activator that mediates resistance to Cu, as well as Zn and Cd. Here, we characterize a novel cysteine-rich domain which is crucial for sensing excess intracellular copper by dMTF-1. Transgenic flies expressing mutant dMTF-1 containing alanine substitutions of two, four or six cysteine residues within the sequence 547CNCTNCKCDQTKSCHGGDC565 are significantly or completely impaired in their ability to protect flies from copper toxicity and fail to up-regulate MtnA (metallothionein) expression in response to excess Cu. In contrast, these flies exhibit wild-type survival in response to copper deprivation thus revealing that the cysteine cluster domain is required only for sensing Cu load by dMTF-1. Parallel studies show that the isolated cysteine cluster domain is required to protect a copper-sensitive S. cerevisiae ace1Δ strain from copper toxicity. Cu(I) ligation by a Cys-rich domain peptide fragment drives the cooperative assembly of a polydentate [Cu4-S6] cage structure, characterized by a core of trigonally S3 coordinated Cu(I) ions bound by bridging thiolate ligands. While reminiscent of Cu4-L6 (L = ligand) tetranuclear clusters in copper regulatory transcription factors of yeast, the absence of significant sequence homology is consistent with convergent evolution of a sensing strategy particularly well suited for Cu(I)

Copper(II)-benzotriazole coordination compounds in click chemistry: a diagnostic reactivity study

This diagnostic study aims to shed light on the catalytic activity of a library of Cu(II) based coordination compounds with benzotriazole-based ligands. We report herein the synthesis and characterization of five new coordination compounds formulated [CuII(L4)(MeCN)2(CF3SO3)2] (1), [CuII(L5)2(CF3SO3)2] (2), [CuII(L6)2(MeCN)(CF3SO3)]·(CF3SO3) (3), [CuII(L6)2(H2O)(CF3SO3)]·(CF3SO3)·2(Me2CO) (4), [CuI4(L1)2(L1’)2(CF3SO3)2]2·4(CF3SO3)·8(Me2CO) (5), derived from similar nitrogen-based ligands. The homogeneous catalytic activity of these compounds along with our previously reported coordination compounds (6 -13), derived from similar ligands, is tested against the well-known Cu(I)-catalysed azide-alkyne cycloaddition reaction. The optimal catalyst [CuII(L1)2(CF3SO3)2] (10) activates the reaction to afford 1,4-disubstituted 1,2,3-triazoles with yields up to 98% and without requiring a reducing agent. Various control experiments are performed to optimize the method as well as examine parameters such as ligand variation, metal coordination geometry and environment, in order to elucidate the behaviour of the catalytic system