A study of the cooperative-office practice training programs in the high schools of Puerto Rico

Thesis (Ed.M.)--Boston Universit

Two phase residence time distribution in a modified twin screw extruder

Biomass fractionation is performed with a modified Clextral twin-screw extruder used as a thermo-mechano-chemical reactor. This new process is firstly analyzed. Visual observations, residence time distributions, and global mass balances are used to obtain information about the process phenomena and their coupling. Residence time distributions (RTD) classical models are adopted to represent the experimental plots. The influence of continuous and discrete process parameters upon the RTD of the solid and liquid phases is analyzed

Spatial Analysis of Land Use by Cattle Herds in a Village of the Sudanese Zone in Senegal. Application for Grazing System Improvement

Spatial analysis of land use by cattle herds in the sub-humid area of Senegal is conducted through the utilisation of a Geographic Information System. This tool allows us to establish relationships between spatial practices, ruminant nutrition and performances. It gives leads to proposals for the improvement of the extensive ruminant feeding system

Quinolinate synthase, an iron-sulfur enzyme in NAD biosynthesis

International audienceNicotinamide adenine dinucleotide (NAD) plays a crucial role as a cofactor in numerous essential redox biological reactions. NAD derives from quinolinic acid which is synthesized in E. coli from L-aspartate and dihydroxyacetone phosphate (DHAP) as the result of the concerted action of two enzymes, L-aspartate oxidase (NadB) and quinolinate synthetase (NadA). We report here the characterization of NadA protein from E. coli. When anaerobically purified, the isolated soluble protein contains 3-3.5 iron and 3-3.5 sulfide/ polypeptide chain. Mössbauer spectra of the 57Fe-protein revealed that the majority of the iron is in the form of a (4Fe-4S)2+ cluster. An enzymatic assay for quinolinate synthetase activity was set up and allowed to demonstrate that the cluster is absolutely required for NadA activity. Exposure to air leads to degradation of the cluster and inactivate enzyme

The crystal structure of Fe₄S₄ quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad.

International audienceQuinolinate synthase (NadA) is a Fe4S4 cluster-containing dehydrating enzyme involved in the synthesis of quinolinic acid (QA), the universal precursor of the essential nicotinamide adenine dinucleotide (NAD) coenzyme. A previously determined apo NadA crystal structure revealed the binding of one substrate analog, providing partial mechanistic information. Here, we report on the holo X-ray structure of NadA. The presence of the Fe4S4 cluster generates an internal tunnel and a cavity in which we have docked the last precursor to be dehydrated to form QA. We find that the only suitably placed residue to initiate this process is the conserved Tyr21. Furthermore, Tyr21 is close to a conserved Thr-His-Glu triad reminiscent of those found in proteases and other hydrolases. Our mutagenesis data show that all of these residues are essential for activity and strongly suggest that Tyr21 deprotonation, to form the reactive nucleophilic phenoxide anion, is mediated by the triad. NadA displays a dehydration mechanism significantly different from the one found in archetypical dehydratases such as aconitase, which use a serine residue deprotonated by an oxyanion hole. The X-ray structure of NadA will help us unveil its catalytic mechanism, the last step in the understanding of NAD biosynthesis

Direct repair of a synthetic 5S-configured spore photoproduct by a spore photoproduct lyase.

International audienceThe spore photoproduct lyase is a Fe-S/AdoMet DNA repair enzyme, which directly repairs spore lesions, induced by UV irradiation of spores, using an unknown radical mechanism. The air sensitive radical SAM enzyme was for the first time challenged with synthetically pure substrates. It was found that the enzyme recognizes a synthetic 5S-configured spore lesion without the central phosphodiester bond. The 5R-configured lesion is in contrast to current belief not a substrate

Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions

Adenosine is undoubtedly an ancient biological molecule that is a component of many enzyme cofactors: ATP, FADH, NAD(P)H, and coenzyme A, to name but a few, and, of course, of RNA. Here we present an overview of the role of adenosine in its most reactive form: as an organic radical formed either by homolytic cleavage of adenosylcobalamin (coenzyme B 12 , AdoCbl) or by single-electron reduction of S -adenosylmethionine (AdoMet) complexed to an iron–sulfur cluster. Although many of the enzymes we discuss are newly discovered, adenosine's role as a radical cofactor most likely arose very early in evolution, before the advent of photosynthesis and the production of molecular oxygen, which rapidly inactivates many radical enzymes. AdoCbl-dependent enzymes appear to be confined to a rather narrow repertoire of rearrangement reactions involving 1,2-hydrogen atom migrations; nevertheless, mechanistic insights gained from studying these enzymes have proved extremely valuable in understanding how enzymes generate and control highly reactive free radical intermediates. In contrast, there has been a recent explosion in the number of radical-AdoMet enzymes discovered that catalyze a remarkably wide range of chemically challenging reactions; here there is much still to learn about their mechanisms. Although all the radical-AdoMet enzymes so far characterized come from anaerobically growing microbes and are very oxygen sensitive, there is tantalizing evidence that some of these enzymes might be active in aerobic organisms including humans.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/69165/1/604_ftp.pd

Tracking the hydro-climatic signal from lake to sediment: a field study from central Turkey

Palaeo-hydrological interpretations of lake sediment proxies can benefit from a robust understanding of the modern lake environment. In this study, we use Nar Gölü, a non-outlet, monomictic maar lake in central Turkey, as a field site for a natural experiment using observations and measurements over a 17-year monitoring period (1997–2014). We compare lake water and sediment trap data to isotopic, chemical and biotic proxies preserved in its varved sediments. Nar Gölü underwent a 3 m lake-level fall between 2000 and 2010. δ18Olakewater is correlated with this lake-level fall, responding to the change in water balance. Endogenic carbonate is shown to precipitate in isotopic equilibrium with lake water and there is a strong relationship between δ18Olakewater and δ18Ocarbonate, which suggests the water balance signal is accurately recorded in the sediment isotope record. Over the same period, sedimentary diatom assemblages also responded, and conductivity inferred from diatoms showed a rise. Shifts in carbonate mineralogy and elemental chemistry in the sediment record through this decade were also recorded. Intra-annual changes in δ18Olakewater and lake water chemistry are used to demonstrate the seasonal variability of the system and the influence this may have on the interpretation of δ18Ocarbonate. We use these relationships to help interpret the sedimentary record of changing lake hydrology over the last 1725 years. Nar Gölü has provided an opportunity to test critically the chain of connection from present to past, and its sedimentary record offers an archive of decadal- to centennial-scale hydro-climatic chang