Escherichia coli synthesizes at least three [NiFe]-hydrogenase enzymes that catalyze the production or consumption of hydrogen gas and occupy a central place in cellular energy metabolism (4, 17). Multiple accessory proteins are required for the assembly of the bimetallic catalytic cluster of these enzymes, including the proteins encoded by the hyp genes and slyD (3, 7, 12). SlyD, which contributes to the insertion of nickel into the hydrogenase precursor proteins and cellular nickel accumulation (18), consists of a peptidyl-prolyl isomerase (PPIase) domain as well as a molecular chaperone domain and a C-terminal tail rich in metal-binding residues (10, 14, 15). A combination of in vitro and in vivo experiments demonstrated that both the metal-binding domain and the chaperone activity of SlyD are essential components of its function in hydrogenase production (13), but the role of SlyDs PPIase activity in the hydrogenase maturation pathway was unknown.. The crystal structure of Methanococcus ...
Cyanobacteria are a heterogeneous group of phototrophic microorganisms. Many cyanobacteria have the capacity to fix atmospheric nitrogen. During the process of nitrogen fixation, molecular hydrogen is produced. Three enzymes are directly involved in hydrogen metabolism in cyanobacteria. A nitrogenase, evolving hydrogen during nitrogen-fixation, an uptake hydrogenase, recycling the hydrogen produced by nitrogenase, and a bidirectional hydrogenase that has the capacity to both take up and produce hydrogen. The main objective in this thesis was to examine the transcriptional regulation of both the uptake and the bidirectional hydrogenase in filamentous cyanobacteria.. The transcriptional regulation of the uptake hydrogenase was demonstrated to be influenced by external conditions in Nostoc muscorum and Nostoc punctiforme. Nickel, molecular hydrogen, and anaerobic conditions all induced the relative amount of uptake hydrogenase transcript. In addition, a transcript could be detected in ...
The native ability of Clostridium thermocellum to rapidly consume cellulose and produce ethanol makes it a leading candidate for a consolidated bioprocessing (CBP) biofuel production strategy. C. thermocellum also synthesizes lactate, formate, acetate, H2, and amino acids that compete with ethanol production for carbon and electrons. Elimination of H2 production could redirect carbon flux towards ethanol production by making more electrons available for acetyl coenzyme A reduction to ethanol. H2 production in C. thermocellum is encoded by four hydrogenases. Rather than delete each individually, we targeted hydrogenase maturase gene hydG, involved in converting the three [FeFe] hydrogenase apoenzymes into holoenzymes. Further deletion of the [NiFe] hydrogenase (ech) resulted in a mutant that functionally lacks all four hydrogenases. H2 production in ∆hydG∆ech was undetectable, and the ethanol yield nearly doubled to 64% of the maximum theoretical yield. Genomic analysis of ∆hydG revealed a mutation
A series of pendant amine-containing [FeFe]-hydrogenase models, [X(CH2S-μ)2{Fe(CO)3}{Fe(CO)(P2 PhN2 Bn)}] (1H, X = CH2; 2Me, C(CH3)2; 3Et, C(CH2CH3)2; and P2 PhN2 Bn = 1,5-dibenzyl-3,7-diphenyl-1,5-diaza-3,7-diphosphacyclooctane) with different groups at the bridgehead carbon of the S-to-S linker were synthesized. The oxidations of these complexes as well as the reverse reduction reaction were studied by cyclic voltammetry and in situ IR spectroscopy. Regardless of the bridgehead steric bulk, all three complexes demonstrate intramolecular iron-mediated C(sp3)-H bond heterolytic cleavage with the assistance of the pendant amine base within the chelating diphosphine ligand in the two-electron oxidation process. X-ray crystallographic analysis shows that the doubly oxidized products, [1′H]+, [2′Me]+, and [3′Et]+, all have a rigid FeSC three-membered ring at the open apical site of the rotated iron center. The most noticeable difference in structures of the oxidized complexes is that the ...
The light-driven splitting of water into its constituting elements gives access to a valuable fuel from an abundant substrate, using sunlight as the only energy source. Synthetic diiron complexes as functional models of the [FeFe] hydrogenase H(2)ase enzyme active site have moved into the centre of focus as potentially viable catalysts for the reductive side of this process, i.e. the reduction of protons to molecular hydrogen. The active site of the enzyme, as well as its mimics in an artificial system, are required to accumulate two electrons from single electron transfer events and to combine them with two protons to form hydrogen. Whereas in biology this reaction is not coupled to photosynthesis and thus proceeds in the dark, additional aspects need to be considered when designing a functional artificial system for the light-driven reduction of protons. Suitable photosensitizers have to be chosen that not only provide sufficient driving force for the reduction of the synthetic diiron ...
TY - JOUR. T1 - Single-Amino Acid Modifications Reveal Additional Controls on the Proton Pathway of [FeFe]-Hydrogenase. AU - Cornish, Adam J.. AU - Ginovska, Bojana. AU - Thelen, Adam. AU - Da Silva, Julio C S. AU - Soares, Thereza A.. AU - Raugei, Simone. AU - Dupuis, Michel. AU - Shaw, Wendy J.. AU - Hegg, Eric L.. PY - 2016/6/7. Y1 - 2016/6/7. N2 - The proton pathway of [FeFe]-hydrogenase is essential for enzymatic H2 production and oxidation and is composed of four residues and a water molecule. A computational analysis of this pathway in the [FeFe]-hydrogenase from Clostridium pasteurianum revealed that the solvent-exposed residue of the pathway (Glu282) forms hydrogen bonds to two residues outside of the pathway (Arg286 and Ser320), implying that these residues could function in regulating proton transfer. In this study, we show that substituting Arg286 with leucine eliminates hydrogen bonding with Glu282 and results in an ∼3-fold enhancement of H2 production activity when methyl ...
Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H2 activation. This finding may stimulate the ongoing synthesis of ...
The effects of cyanide on membrane-associated and purified hydrogenase from Azotobacter vinelandii were characterized. Inactivation of hydrogenase by cyanide was dependent on the activity (oxidation) state of the enzyme. Active (reduced) hydrogenase showed no inactivation when treated with cyanide over several hours. Treatment of reversibly inactive (oxidized) states of both membrane-associated and purified hydrogenase, however, resulted in a time-dependent, irreversible loss of hydrogenase activity. The rate of cyanide inactivation was dependent on the cyanide concentration and was an apparent first-order process for purified enzyme (bimolecular rate constant, 23.1 M{sup {minus}1} min{sup {minus}1} for CN{sup {minus}}). The rate of inactivation decreased with decreasing pH. ({sup 14}C)cyanide remained associated with cyanide-inactivated hydrogenase after gel filtration chromatography, with a stoichiometry of 1.7 mol of cyanide bound per mol of inactive enzyme. The presence of saturating ...
Transcription of the hupSL genes, which encode the uptake [NiFe]hydrogenase of Rhodobacter capsulatus, is specifically activated by H2. Three proteins are involved, namely the H2-sensor HupUV, the histidine kinase HupT and the transcriptional activator HupR. hupT and hupUV mutants have the same phenotype, i.e. an increased level of hupSL expression (assayed by phupS::lacZ fusion) in the absence of H2; they negatively control hupSL gene expression. HupT can autophosphorylate its conserved His217, and in vitro phosphotransfer to Asp54 of its cognate response regulator, HupR, was demonstrated. The non-phosphorylated form of HupR binds to an enhancer site (5′-TTG-N5-CAA) of phupS localized at −162/−152 nt and requires integration host factor to activate fully hupSL transcription. HupUV is an O2-insensitive [NiFe]hydrogenase, which interacts with HupT to regulate the phosphorylation state of HupT in response to H2 availability. The N-terminal domain of HupT, encompassing the PAS domain, is ...
Proton channels facilitate the movement of protons over large distances and are critical in many reactions, from controlling proton delivery in metalloenzymes[1] to moving protons through PEM fuel cells.[2] Hydrogenases are enzymes that use proton channels to deliver protons to or from the enzyme active site to achieve high rates of hydrogen production and oxidation at low overpotentials.[3] The [Ni(PR2NR2)2]2+ series of complexes, which are functional mimics of the [FeFe]-hydrogenase active site, utilize pendant amines to move the proton to or from the Ni, resulting in some of the fastest synthetic catalysts for hydrogen production and oxidation reported.[4] While intramolecular proton movement has been shown to be facile,[5] deprotonation of hydrogen oxidation catalysts can be a slow step for catalysis.[6] Additionally, a stable H2 adduct (endo-endo) is formed which, if bypassed, could contribute to an overall enhanced rate (Figure 1). A proton channel may aid in addressing these outstanding ...
Hydrogenase enzymes are natures catalysts for hydrogen production and uptake. Understanding how they work may lead to new materials as alternatives for precious metals currently used in H2-utilizing fuel and producer cells. Work described in this thesis focuses on synthetic mimics of the active site of [Fe Fe]-hydrogenases and explores their reactivity towards protons and electrons. Chapter 1 gives a brief overview of the chemistry taking place in hydogenase enzymes with a particular focus on the [Fe Fe]-hydrogenase. The evolution of synthetic models mimicking the structure and function of the enzyme from the late 1990s to the current state of the art is discussed. Chapter 2 describes synthesis of the first {2Fe3S} hydride together with new active site mimics in which bulky substituents are incorporated into the dithiolate bridgehead. A comprehensive examination of their structural features and spectroscopic properties is provided. Chapter 3 reports extensive stopped-flow UV-vis, IR and ...
Introductory report: distribution and physiological role of hydrogenases in microorganisms. Characterization of iron-sulphur centres by EPR spectroscopy: comparison with model systems. Hydrogenase in strictly anaerobic bacteria. Structure and function of two hydrogenases from the dinitrogen-fixing bacterium Clostridium pasteurianum. Activity, acceptor specificity and function of hydrogenase in Methanobacterium thermoautotrophicum. Characterization of the periplasmic hydrogenase from Desulfovibrio gigas. Properties of hydrogenase from particulate fraction of Desulfovibrio vulgaris. Properties of hydrogenases from the anaerobic bacteria Megasphera elsdenii and Desulfovibrio vulgaris. Hydrogenase in anaerobic phototrophic bacteria. Nature of the iron sulfur core and stability of chromatium hydrogenase. Purification and some properties of the soluble part of hydrogenase from Chromatium vinosum. Physical and catalytic properties of the hydrogenase of Rhodospirillum rubrum. Comparison of properties ...
Angewandte Chemie DOI: 10.1002/ange.201006255 H2 Activation Iron-Chromophore Circular Dichroism of [Fe]-Hydrogenase: The Conformational Change Required for H2 Activation** Seigo Shima,* Sonja Vogt, Andreas Gbels, and Eckhard Bill Circular dichroism (CD) spectroscopy is a very sensitive method used to detect changes in inherently chiral chromophores and in achiral chromophores embedded in chiral surroundings.[1] Information on the secondary structures of proteins can be obtained by CD spectroscopy in the far-UV spectral region (190-250 nm), and CD in the near-UV region (250-350 nm) can be sensitive to certain aspects of tertiary structure.[1b] Near-UV and visible CD spectroscopy is also used to analyze metal complexes[1a,c] and the active site of metal-containing enzymes, such as P450 (300-500 nm), galactose oxidase (300-700 nm), and biotin sulfoxide reductase (300-650 nm).[2] The [Fe]-hydrogenase found in many methanogenic archaea catalyzes the reversible reduction of ...
The process of N fixation is energy consuming and inefficient. In most cases 20 to 40% of the energy that is supplied to nitrogenase for the reduction of N2 is utilized for the reduction of protons to H2. Some strains of R. japonicum contain a membrane-bound hydrogenase that is capable of oxidizing all of the H2 that is produced during N2 fixation. This study was conducted to evaluate the effects of inoculation of soybeans [Glycine max (L.) Merr.] with Rhizobium japonicum containing H2 recycling capability on N fixation efficiency and soybean yield at various physiological stages of growth.. In these experiments, a H2-oxidizing strain SR (Hup+) and SR3 (Hup−), a mutant derived from SR which is unable to oxidize H2, were utilized. Soybeans cv. Wilkin were grown under bacteriological conditions utilizing a drip-irrigated nutriculture system. Nodules from plants inoculated with SR evolved no measurable amount of H2, while nodules from plants innoculated with SR3 evolved between 2.7 and 10 ...
Biosynthesis of the Catalytic H-Cluster of [FeFe] Hydrogenase. Abstract. [FeFe] hydrogenase enzymes rapidly evolve H2 at a 6-Fe catalytic site termed the H-cluster, which consists of a traditional [4Fe-4S] cluster linked via a cysteine bridge to a dinuclear Fe subcluster [2Fe]H that possesses unusual biological ligands: two terminal CN- ligands, two terminal CO ligands, and azadithiolate and CO bridges, all of which are thought to be synthesized and installed by a set of Fe-S proteins denoted HydE, HydF, and HydG. With the James Swartz laboratory (Stanford University) we can generate [FeFe] hydrogenase in high yield using cell free synthesis methods, allowing for specific isotope labelling of its components as needed for definitive spectroscopic studies (1).. The radical S-adenosylmethionine (SAM) enzyme HydG lyses free L-tyrosine to produce CO and CN- for the assembly of the H-cluster. We use electron paramagnetic resonance (EPR) spectroscopy to detect and characterize HydG reaction ...
Hydrogenases catalyze the formation of hydrogen. The cofactor (H-cluster) of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H-2-producing catalysts.. ...
Metagenomic and PCR-based diversity surveys of [FeFe]-hydrogenases combined with isolation of alkaliphilic hydrogen-producing bacteria from the serpentinite-hosted Prony hydrothermal field, New Caledonia ...
Metagenomic and PCR-based diversity surveys of [FeFe]-hydrogenases combined with isolation of alkaliphilic hydrogen-producing bacteria from the serpentinite-hosted Prony hydrothermal field, New Caledonia ...
Nickel-containing hydrogenases, the biological catalysts of H-2 oxidation and production, reversibly inactivate under anaerobic, oxidizing conditions. We aim at understanding the mechanism of (in)activation and what determines its kinetics, because there is a correlation between fast reductive reactivation and oxygen tolerance, a property of some hydrogenases that is very desirable from the point of view of biotechnology. Direct electrochemistry is potentially very useful for learning about the redox-dependent conversions between active and inactive forms of hydrogenase, but the voltammetric signals are complex and often misread. Here we describe simple analytical models that we used to characterize and compare 16 mutants, obtained by substituting the position-74 valine of the O-2-sensitive NiFe hydrogenase from Desulfovibrio fructosovorans. We observed that this substitution can accelerate reactivation up to 1,000-fold, depending on the polarity of the position 74 amino acid side chain. In ...
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Lui BH, Cochran JR, Swartz, JR. Discovery of improved EGF agonists using a novel in vitro screening platform. J Mol Biol. 2011 Oct 21;413(2):4 06-15. Epub 2011 Aug 23. PMID 21888916 Yang WC, Welsh JP, Lee J, Cooke JP, Swartz JR. Solubility partner IF2 Domain I enables high yield synthesis of transducible transcription factors in Escherichia coli. Protein Expr Purif. 2011 Nov;80(1):145-51. doi: 10.1016/j.pep.2011.06.017. Epub 2011 Jul 2. PMID 21757009 Kuchenreuther JM, George SJ, Grady-Smith CS, Cramer SP, Swartz JR. Cell-free H-cluster synthesis and [FeFe] hydrogenase activation: all five CO and CN⁻ ligands derive from tyrosine. PLoS One (2011);6(5):e20346. Epub 2011 May 31. PMID 21673792 Bingham AS, Smith PR, Swartz JR. Evolution of an [FeFe] hydrogenase with decreased oxygen sensitivity. International Journal of Hydrogen Energy (2011) doi:10.1016/j.ijhydene.2011.02.048 Smith PR, Bingham AS, Swartz JR. Generation of hydrogen from NADPH using an [FeFe] hydrogenase. International Journal of ...
Lui BH, Cochran JR, Swartz, JR. Discovery of improved EGF agonists using a novel in vitro screening platform. J Mol Biol. 2011 Oct 21;413(2):4 06-15. Epub 2011 Aug 23. PMID 21888916 Yang WC, Welsh JP, Lee J, Cooke JP, Swartz JR. Solubility partner IF2 Domain I enables high yield synthesis of transducible transcription factors in Escherichia coli. Protein Expr Purif. 2011 Nov;80(1):145-51. doi: 10.1016/j.pep.2011.06.017. Epub 2011 Jul 2. PMID 21757009 Kuchenreuther JM, George SJ, Grady-Smith CS, Cramer SP, Swartz JR. Cell-free H-cluster synthesis and [FeFe] hydrogenase activation: all five CO and CN⁻ ligands derive from tyrosine. PLoS One (2011);6(5):e20346. Epub 2011 May 31. PMID 21673792 Bingham AS, Smith PR, Swartz JR. Evolution of an [FeFe] hydrogenase with decreased oxygen sensitivity. International Journal of Hydrogen Energy (2011) doi:10.1016/j.ijhydene.2011.02.048 Smith PR, Bingham AS, Swartz JR. Generation of hydrogen from NADPH using an [FeFe] hydrogenase. International Journal of ...
FUNCTIONAL GENOMIC EXPRESSIONS OF Fe-ONLY HYDROGENASE AND Ni-Fe HYDROGENASE FOR THE PREPARATION OF BACTERIA AND ARCHEA SPECIES ANAEROBIC SEED SLUDGE FAVOURING SOLVENTOGENESIS HYDROGENESIS AND METHANOGENESIS PROCESSES FOR THE ENHANCED PRODUCTION OF ETHANOL, HYDROGEN AND METHANE.. Microbial Morphology, Community Structure and Phylogenesis and Functional of Hydrogeniser and Methaniser Using PCR.. ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Clostridium thermocellum has the ability to catabolize cellulosic biomass into ethanol, but acetic acid, lactic acid, carbon dioxide, and hydrogen gas (H2) are also produced. The effect of hydrogenase
Hydrogenase-1 (Hyd-1) from Escherichia coli is a membrane-bound enzyme that catalyses the reversible oxidation of molecular H2. The active site contains one Fe and one Ni atom and several conserved amino acids including an arginine (Arg509), which interacts with two conserved aspartate residues (Asp118 and Asp574) forming an outer shell canopy over the metals. There is also a highly conserved glutamate (Glu28) positioned on the opposite side of the active site to the canopy. The mechanism of hydrogen activation has been dissected by site-directed mutagenesis to identify the catalytic base responsible for splitting molecular hydrogen and possible proton transfer pathways to/from the active site. Previous reported attempts to mutate residues in the canopy were unsuccessful, leading to an assumption of a purely structural role. Recent discoveries, however, suggest a catalytic requirement, for example replacing the arginine with lysine (R509K) leaves the structure virtually unchanged, but catalytic ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
In the background to the following speculation we still have a FeNi hydrogenase "visiting" a proton channeling pore to generate reduced ferredoxin using a localised low pH region just inside the cell. In the archaea Im assuming there is no preformed Na+ pump because the protein translocating precursor never jammed up so never pumped Na+ ions. There was no drop in intracellular Na+ and the FeNi hydrogenase never attached firmly to the proton pore in the membrane. Interestingly the methanogens do still have a cytoplasmic FeNi hydrogenase (or NiFe in this illustration) passing electrons down FeS wires. Instead of dropping them straight on to ferredoxin to generate reduced Fd2- using the proton gradient of the cell wall conducted through a membrane pore (as per proto Ech), pairs of electrons are split at an FAD. Half do the up hill job of generating Fd2- and the other half tumble down hill to the easy target of heterodisulphide. Energy from the latter down hill reaction is used to allow the up hill ...
HypC; accessory protein necessary for maturation of the hydrogenase isoforms 1, 2 and 3; forms a complex with HypD, HypE, and HypF proteins, which is the site of ligand biosynthesis and attachment to the iron atom of the NiFe site in the hydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology (90 aa ...
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95. C. Lambertz, N. Leidel, K. Havelius, P. Chernev, J. Noth, M. Winkler, T. Happe, M. Haumann, O2 reactions at the six-iron active site (H-cluster) of [FeFe]-hydrogenase. J. Biol. Chem. 286, 40614-40623 (2011). 94. N. Planas, L. Vigara, C. Cady, P. Miro, P. Huang, L. Hammarström, S. Styring, N. Leidel, H. Dau, M. Haumann, L. Gagliardi, C. J. Cramer, A. Llobet, Electronic structure of oxidized complexes derived from cis-[RuII(bpy)2(H2O)2]2+ and its photoisomerization mechanism. Inorg. Chem. 50, 11134-11142 (2011). 93. P. P. Samuel, A. Döring, S. Horn, K. Havelius, S. Reschke, L. Leimkühler, M. Haumann, C. Schulzke, A crystallographic and Mo K-edge XAS study of molybdenum-oxo bis-, mono-, and non-dithiolene complexes: first-sphere coordination and non-innocence of ligands. Eur. J. Inorg. Chem. 28, 4387-4399 (2011). 92. J. Fritsch, S. Löscher, O. Sanganas, E. Siebert, I. Zebger, M. Ludwig, M. Stein, A. De Lacey, H. Dau, B. Friedrich, O. Lenz, M. Haumann, NiFe and FeS cofactors in ...
Genetic information processingProtein fateProtein modification and repair[FeFe] hydrogenase H-cluster maturation GTPase HydF (TIGR03918; HMM-score: 17.7) ...
We describe a general microscopic model for the calculation of diffusion and binding rates of small ligands (e.g. gas molecules) to protein active sites [1-3]. In our model, the diffusive hopping of the ligand within the protein is coarse grained using a master equation approach with transition rates between the coarse states (= protein cavities) estimated from equilibrium and non-equilibrium molecular dynamics simulations and density functional theory for the final chemical binding step. The master equation is propagated to obtain the ligand population of the active site as a function of time. A fit of the time-dependent populations to a phenomenological rate law gives the phenomenological diffusion rate constants that can be compared to experimental measurements. We report the application of this methodology to a number of enzymes that have recently attracted much interest for biotechnological applications such as H2 oxidation and production in biofuel cells ([NiFe]-hydrogenase) [1,2] as well ...
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I think it is useful to recall the relevant historical timeline.. The connection between axial-gravitational anomaly and transport (in flat space) at finite temperature, zero chemical potential was first suggested in a paper by Landsteiner, Megías, and Pena-Benitez, https://arxiv.org/abs/1103.5006. The effect was first pointed out to be possible by Neiman and Oz (arXiv:1011.5107). Landsteiner et al. suggested that the coefficient of this effect is equal to the coefficient of axial-gravitational anomaly, multiplied by temperature squared. How did they know? They constructed a simple theory in AdS5 so that the corresponding CFT4 has an axial-gravitational anomaly. Then they considered a black-brane solution, and by using AdS/CFT, found a "chiral vortical" coefficient proportional to the coefficient of the axial-gravitational anomaly.. I remember being very perplexed by the claimed connection between transport in flat space and anomaly in curved space appeared to me very strange. Not only that ...
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Now if you are feeling a little skeptical, allow me to assure you this. From cereal boxes to weight-loss classes, the carbo-heavy food pyramid is all the feel good report. According to the American … ...
Ive seen this bag featured as the new It bag in more magazines than I can count... Harpers (I think) even did a huge spread on how it would...
Last week, we noted along with many news outlets that a biomarker had been apparently discovered for PTSD. The researchers claimed they had a new tool to help
You could tell that Charlie Ward is all keyed up over the approaching FSU-Florida game because he was speaking almost loud enough to be heard.The gifted, but remarkably unaffected FSU quarterback
Forget about all the hype. We reviewed Alpha Brain and here are the results. We break down its ingredients, clinical trials and much, much more!
In the end, much of the hype surrounding the FCCs meeting this week amounted to nothing. After a delay of almost 12-hours, the meeting opened with a diminished...
As some enterprises find the reality of cloud fails to live up to the hype, Clive Longbottom explains why serverless computing could help firms attain the operational benefits theyre looking for
It seems like everything these days is considered a superfood, so we decided to look into which of these foods are actually research-backed and which ones are all hype.
As of now it appears all the hype over the Swine Flu maybe not pan out to meet the news agencies expectations but lessons learned here can and should be
Previous studies have showed that the hydrogen gas evolved from Hup - legume nodules promotes plant growth and increases the hydrogen uptake rate of soils adjacent to Hup - nodules. This may be resulted from hydrogen-induced variation of rhizobacterial community structure. Twenty isolates of hydrogen-oxidizing bacteria belonging to genera of Variovorax, Burkhorderia and Flavobacterium showed positive effect on root elongation. This study showed that isolates belonging to Variovorax and Flavobacterium had ACC deaminase activity and isolates belonging to Burkhorderia had the ability to excrete rhizobitoxine or its structural analogue such as AVG, which meant that they have the ability to promote plant growth by lowering of plant ethylene levels. TRFLP studies showed that hydrogen metabolism resulted in obvious variation of bacterial community structure in hydrogen treated soils compared to the controls. TRF peaks whose intensity increased obviously in profiles from hydrogen-treated soils were ...