High Percentages of Reclaimed Asphalt Affect the Performance of Asphalt Binder

More than 90 percent of the road and highway network in the United States is paved with asphalt concrete. Maintenance and periodic rehabilitation require a continuous supply of aggregates and asphalt binder, both of which are becoming increasingly scarce and expensive. Recycling and reusing these resources can reduce costs and improve sustainability. The most common recyclable material used in road construction is reclaimed asphalt pavement (RAP), which is milled asphalt surface layers that have been removed from existing pavements before new asphalt overlay is placed. Reclaimed asphalt roofing shingles (RAS) are another potential source of asphalt binder.There is growing interest in allowing significantly higher percentages of RAP and RAS in asphalt mixes used on state and local roadways. However, making this change has raised concerns regarding how these composite binders may influence the performance and durability of asphalt mixes, depending on the blends of different virgin and reused binders. Researchers at the UC Pavement Research Center investigated the use of higher percentages of RAP and RAS as a partial replacement for the virgin binder in new asphalt mixes and their effect on pavement performance in California. This research brief summarizes findings from that study.View the NCST Project Webpag

A perception-action strategy for hummingbirds

Many human and animal tasks are thought to be controlled with the tau informational variable. It is widely accepted that controlling the rate of change of tau during decelerative tasks, such as when braking or landing, is one common perceptual control strategy. However, many tasks require accelerating before decelerating to a goal, such as reaching. An advancement of tau theory shows how a single action formula may be used to control the full action unit from initiation to peak velocity, and to rest at the goal, with the same perceptual tau information as before and accounting for the same decelerative kinematics as before. Here, we test the theory against data from high-speed video of a hummingbird flying to its flower feeder. We find that the theory accounts for 97% of the variance in the data, and thus supports it

The crystal structure of a biological insulated transmembrane molecular wire

A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport electrons between the interior and exterior environments of phylogenetically and metabolically diverse microorganisms. The structure is revealed as a naturally insulated biomolecular wire possessing a 10-heme cytochrome, MtrA, insulated from the membrane lipidic environment by embedding within a 26 strand β-barrel formed by MtrB. MtrAB forms an intimate connection with an extracellular 10-heme cytochrome, MtrC, which presents its hemes across a large surface area for electrical contact with extracellular redox partners, including transition metals and electrodes

Characterisation of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth

The autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidised at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron conduit through the outer membrane. Electrons are then transported to the cytoplasmic membrane where they are used to generate proton motive force (for ATP synthesis) and NADH for autotrophic processes such as carbon fixation. As part of the mtoAB gene cluster, S. lithotrophicus also contains the gene mtoD that is proposed to encode a cytochrome c protein. We isolated mtoD from a Shewanella oneidensis expression system where the mtoD gene was expressed on a pBAD plasmid vector. Biochemical, biophysical and crystallographic characterisation of the purified MtoD revealed it as an 11 kDa monomeric protein containing a single heme. Sequence and structural alignment indicated that MtoD belonged to the class-1 cytochrome c family and had a similar fold to ferricytochrome c552 family, however the MtoD heme is bis-histidine coordinated and is substantially more exposed than the hemes of other family members. The reduction potential of the MtoD heme at pH 7 was +155 mV vs. Standard Hydrogen Electrode, which is approximately 100 mV lower than that of mitochondrial cytochromes c. Consideration of the properties of MtoD in the context of the potential respiratory partners identified from the genome suggests that MtoD could associate to multiple electron transfer partners as the primary periplasmic electron shuttle

Reporting war: Grammar as 'covert operation'

While it is often said that 'truth is the first casualty of war', this aphorism covers only one feature of how wars are reported, namely the deliberate use of misinformation by parties to a war. But language is by its nature a higly plastic resource: there is never just one way to report a set of events, even when the 'facts' may be uncontested. Drawing on data from newspaper reports and media briefings of the recent war in Iraq, we illustarte some of the basic grammtical systems which underlie the choice a journalist has to make, particularly in reporting 'high impact' events of the war. Using a functional apporach to grammar—where grammar is seen not as rules but as a theory of reality— we introduce some basic grammatical concepts or undertsanding the idelogical impact if different gramatical choices in contruing the events of war.&nbsp

Resolution of Key Roles for the Distal Pocket Histidine in Cytochrome c Nitrite Reductases

Cytochrome c nitrite reductases perform a key step in the biogeochemical N-cycle by catalyzing the six-electron reduction of nitrite to ammonium. These multi-heme cytochromes contain a number of His/His ligated c-hemes for electron transfer and a structurally differentiated heme that provides the catalytic center. The catalytic heme has proximal ligation from lysine, or histidine, and an exchangeable distal ligand bound within a pocket that includes a conserved histidine. Here we describe properties of a penta-heme cytochrome c nitrite reductase in which the distal His has been substituted by Asn. The variant is unable to catalyze nitrite reduction despite retaining the ability to reduce a proposed intermediate in that process, namely, hydroxylamine. A combination of electrochemical, structural and spectroscopic studies reveals that the variant enzyme simultaneously binds nitrite and electrons at the catalytic heme. As a consequence the distal His is proposed to play a key role in orienting the nitrite for N-O bond cleavage. The electrochemical experiments also reveal that the distal His facilitates rapid nitrite binding to the catalytic heme of the native enzyme. Finally it is noted that the thermodynamic descriptions of nitrite- and electron-binding to the active site of the variant enzyme are modulated by the prevailing oxidation states of the His/His ligated hemes. This is behavior that is likely to be displayed by other multi-centered redox enzymes such that there are wide implications for considering the determinants of catalytic activity in this important and varied group of oxidoreductases

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

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

Mechanisms of Bacterial Extracellular Electron Exchange.

The biochemical mechanisms by which microbes interact with extracellular soluble metal ions and insoluble redox-active minerals have been the focus of intense research over the last three decades. The process presents two challenges to the microorganism; firstly electrons have to be transported at the cell surface, which in Gram negative bacteria presents an additional problem of electron transfer across the ~ 6 nm of the outer membrane. Secondly the electrons must be transferred to or from the terminal electron acceptors or donors. This review covers the known mechanisms that bacteria use to transport electrons across the cell envelope to external electron donors/acceptors. In Gram negative bacteria electron transfer across the outer membrane involves the use of an outer membrane β-barrel and cytochrome. These can be in the form of a porin-cytochrome protein, such as Cyc2 of Acidothiobacillus ferrioxydans, or a multiprotein porin-cytochrome complex like MtrCAB of Shewanella oneidensis MR-1. For mineral respiring organisms there is the additional challenge of transferring the electrons from the cell to mineral surface. For the strict anaerobe Geobacter sulfurreducens this requires electron transfer through conductive pili to associated cytochrome OmcS that directly reduces Fe(III)oxides, while the facultative anaerobe S. oneidensis MR-1 accomplishes mineral reduction through direct membrane contact, contact through filamentous extentions and soluble flavin shuttles, all of which require the outer membrane cytochromes MtrC and OmcA in addition to secreted flavin

An investigation of harmonic correction techniques using active filtering

This thesis presents an investigation of techniques used to mitigate the undesirable effects of harmonics in power systems. The first part of this research develops an effective and useful comparison of alternative AC-DC converter topologies. In particular, a full evaluation of the circuit first proposed by Enjeti (known here as the Texas circuit) with a capacitively smoothed output voltage is made, specifically for operation as a 'clean power' supply interface for a variable speed drive (VSD). This mode of operation has not previously been reported in research literature. Simulation and experimental results verify the performance of the circuit and demonstrate that it draws a current with low harmonic content, but the circuit has a number of problems. This part of the research concludes that the six-switch rectifier is the most viable circuit for operation as a supply interface for a VSD due to its bidirectional power flow capability and its excellent versatility of performance. The second part of this research exploits the versatility of the six-switch rectifier and develops the current control strategy for operation of the circuit as a sinusoidal frontend and as a shunt active filter. It is found that the 'traditional' current control method suffers a significant drop in performance when the switching frequency is constrained to 2kHz due to high power levels. The major development in this thesis was an advanced current control strategy, where additional rotating frames of reference are introduced, thereby converting previously oscillatory current values to d.c. values. This is demonstrated to result in vastly improved immunity to disturbances such as supply distortion and a greatly improved steady state performance. In addition, the new controller requires no additional circuitry (apart from current transducers on the load current) and can be applied to an existing sinusoidal front end. Simulation results confirm the operation of the controller with the circuit operating as both a shunt active filter and as a sinusoidal front end. The new controller has been implemented on an experimental rig exhibiting the features of a high power inverter, i.e. low switching frequency and significant device turn-on and turn-off times, and the results confirm the superior performance of the new current controller

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

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