5,729 research outputs found

    Leading quantum gravitational corrections to QED

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    We consider the leading post-Newtonian and quantum corrections to the non-relativistic scattering amplitude of charged spin-1/2 fermions in the combined theory of general relativity and QED. The coupled Dirac-Einstein system is treated as an effective field theory. This allows for a consistent quantization of the gravitational field. The appropriate vertex rules are extracted from the action, and the non-analytic contributions to the 1-loop scattering matrix are calculated in the non-relativistic limit. The non-analytical parts of the scattering amplitude are known to give the long range, low energy, leading quantum corrections, are used to construct the leading post-Newtonian and quantum corrections to the two-particle non-relativistic scattering matrix potential for two massive fermions with electric charge.Comment: 14 pages, 29 figures, format RevTex

    A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation

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    In the absence of ammonium, many organisms, including the halophilic archaeon Haloferax volcanii DS2 (DM3757), may assimilate inorganic nitrogen from nitrate or nitrite, using a ferredoxin-dependent assimilatory NO3-/NO2- reductase pathway. The small acidic ferredoxin Hv-Fd plays an essential role in the electron transfer cascade required for assimilatory nitrate and nitrite reduction by the cytoplasmic NarB- and NirA-type reductases respectively. UV–visible absorbance and EPR spectroscopic characterization of purified Hv-Fd demonstrate that this protein binds a single [2Fe–2S] cluster, and potentiometric titration reveals that the cluster shares similar redox properties with those present in plant-type ferredoxins

    Optimality Theory as a Framework for Lexical Acquisition

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    This paper re-investigates a lexical acquisition system initially developed for French.We show that, interestingly, the architecture of the system reproduces and implements the main components of Optimality Theory. However, we formulate the hypothesis that some of its limitations are mainly due to a poor representation of the constraints used. Finally, we show how a better representation of the constraints used would yield better results

    The Crystal Structure of the Extracellular 11-heme Cytochrome UndA Reveals a Conserved 10-heme Motif and Defined Binding Site for Soluble Iron Chelates

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    Members of the genus Shewanella translocate deca- or undeca-heme cytochromes to the external cell surface thus enabling respiration using extracellular minerals and polynuclear Fe(III) chelates. The high resolution structure of the first undeca-heme outer membrane cytochrome, UndA, reveals a crossed heme chain with four potential electron ingress/egress sites arranged within four domains. Sequence and structural alignment of UndA and the deca-heme MtrF reveals the extra heme of UndA is inserted between MtrF hemes 6 and 7. The remaining UndA hemes can be superposed over the heme chain of the decaheme MtrF, suggesting that a ten heme core is conserved between outer membrane cytochromes. The UndA structure has also been crystallographically resolved in complex with substrates, an Fe(III)-nitrilotriacetate dimer or an Fe(III)-citrate trimer. The structural resolution of these UndA-Fe(III)-chelate complexes provides a rationale for previous kinetic measurements on UndA and other outer membrane cytochromes

    Jet-Induced Nucleosynthesis in Misaligned Microquasars

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    The jet axes and the orbital planes of microquasar systems are usually assumed to be approximately perpendicular, eventhough this is not currently an observational requirement. On the contrary, in one of the few systems where the relative orientations are well-constrained, V4641Sgr, the jet axis is known to lie not more than ~36 degrees from the binary plane. Such a jet, lying close to the binary plane, and traveling at a significant fraction of the speed of light may periodically impact the secondary star initiating nuclear reactions on its surface. The integrated yield of such nuclear reactions over the age of the binary system (less the radiative mass loss) will detectably alter the elemental abundances of the companion star. This scenario may explain the anomalously high Li enhancements (roughly ~20-200 times the sun's photospheric value; or, equivalently, 0.1-1 times the average solar system value) seen in the companions of some black-hole X-ray binary systems. (Such enhancements are puzzling since Li nuclei are exceedingly fragile - being easily destroyed in the interiors of stars - and Li would be expected to be depleted rather than enhanced there.) Gamma-ray line signatures of the proposed process could include the 2.22 MeV neutron capture line as well as the 0.478 MeV 7Li* de-excitation line, both of which may be discernable with the INTEGRAL satellite if produced in an optically thin region during a large outburst. For very energetic jets, a relatively narrow neutral pion gamma-decay signature at 67.5 MeV could also be measurable with the GLAST satellite. We argue that about 10-20% of all microquasar systems ought to be sufficiently misaligned as to be undergoing the proposed jet-secondary impacts.Comment: ApJ, accepted. Includes referee's suggestions and some minor clarifications over previous versio

    Comparative structure-potentio-spectroscopy of the Shewanella outer membrane multiheme cytochromes

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    Many species of bacteria can generate energy in the anoxic subsurface by directly coupling intracellular oxidative reactions to the reduction of extracellular metal oxides. Coupling these processes requires electron transfer networks that extend from the inside of the cell, across the outer membrane to the extracellular terminal electron acceptors. The best described of these networks is from Shewanella oneidensis MR-1, where four structures of outer membrane multiheme cytochromes (OMMCs) have been determined. These OMMCs contain 10-11 bis-histidine ligated c-type hemes and are directly involved in the reduction of iron and manganese oxides at the cell surface. The heme ligands for some of these structures have been characterised using electron paramagnetic resonance (EPR), the redox-properties have been mapped by protein film electrochemistry (PFE) and more recently molecular dynamic simulations have been used to obtain microscopic redox potentials for individual heme groups. This review maps these different experimental techniques onto the structures, providing insight into the intramolecular electron transfer pathways of OMMCs, revealing future directions for study

    A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella

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    CymA (tetrahaem cytochrome c) is a member of the NapC/NirT family of quinol dehydrogenases. Essential for the anaerobic respiratory flexibility of shewanellae, CymA transfers electrons from menaquinol to various dedicated systems for the reduction of terminal electron acceptors including fumarate and insoluble minerals of Fe(III). Spectroscopic characterization of CymA from Shewanella oneidensis strain MR-1 identifies three low-spin His/His co-ordinated c-haems and a single high-spin c-haem with His/H2O co-ordination lying adjacent to the quinol-binding site. At pH 7, binding of the menaquinol analogue, 2-heptyl-4-hydroxyquinoline-N-oxide, does not alter the mid-point potentials of the high-spin (approximately −240 mV) and low-spin (approximately −110, −190 and −265 mV) haems that appear biased to transfer electrons from the high- to low-spin centres following quinol oxidation. CymA is reduced with menadiol (Em=−80 mV) in the presence of NADH (Em=−320 mV) and an NADH–menadione (2-methyl-1,4-naphthoquinone) oxidoreductase, but not by menadiol alone. In cytoplasmic membranes reduction of CymA may then require the thermodynamic driving force from NADH, formate or H2 oxidation as the redox poise of the menaquinol pool in isolation is insufficient. Spectroscopic studies suggest that CymA requires a non-haem co-factor for quinol oxidation and that the reduced enzyme forms a 1:1 complex with its redox partner Fcc3 (flavocytochrome c3 fumarate reductase). The implications for CymA supporting the respiratory flexibility of shewanellae are discussed.</jats:p

    "Liquid-like" Water in Clathrates Induced by Host-Guest Hydrogen Bonding

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