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hydrogenase</title> <meta name="description" content="Search results for: hydrogenase"> <meta name="keywords" content="hydrogenase"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none navbar-toggler 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id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="hydrogenase"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 6</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: hydrogenase</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">6</span> De Novo Design of a Minimal Catalytic Di-Nickel Peptide Capable of Sustained Hydrogen Evolution </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Saroj%20Poudel">Saroj Poudel</a>, <a href="https://publications.waset.org/abstracts/search?q=Joshua%20Mancini"> Joshua Mancini</a>, <a href="https://publications.waset.org/abstracts/search?q=Douglas%20Pike"> Douglas Pike</a>, <a href="https://publications.waset.org/abstracts/search?q=Jennifer%20Timm"> Jennifer Timm</a>, <a href="https://publications.waset.org/abstracts/search?q=Alexei%20Tyryshkin"> Alexei Tyryshkin</a>, <a href="https://publications.waset.org/abstracts/search?q=Vikas%20Nanda"> Vikas Nanda</a>, <a href="https://publications.waset.org/abstracts/search?q=Paul%20Falkowski"> Paul Falkowski</a> </p> <p class="card-text"><strong>Abstract:</strong></p> On the early Earth, protein-metal complexes likely harvested energy from a reduced environment. These complexes would have been precursors to the metabolic enzymes of ancient organisms. Hydrogenase is an essential enzyme in most anaerobic organisms for the reduction and oxidation of hydrogen in the environment and is likely one of the earliest evolved enzymes. To attempt to reinvent a precursor to modern hydrogenase, we computationally designed a short thirteen amino acid peptide that binds the often-required catalytic transition metal Nickel in hydrogenase. This simple complex can achieve hundreds of hydrogen evolution cycles using light energy in a broad range of temperature and pH. Biophysical and structural investigations strongly indicate the peptide forms a di-nickel active site analogous to Acetyl-CoA synthase, an ancient protein central to carbon reduction in the Wood-Ljungdahl pathway and capable of hydrogen evolution. This work demonstrates that prior to the complex evolution of multidomain enzymes, early peptide-metal complexes could have catalyzed energy transfer from the environment on the early Earth and enabled the evolution of modern metabolism <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hydrogenase" title="hydrogenase">hydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=prebiotic%20enzyme" title=" prebiotic enzyme"> prebiotic enzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=metalloenzyme" title=" metalloenzyme"> metalloenzyme</a>, <a href="https://publications.waset.org/abstracts/search?q=computational%20design" title=" computational design"> computational design</a> </p> <a href="https://publications.waset.org/abstracts/138342/de-novo-design-of-a-minimal-catalytic-di-nickel-peptide-capable-of-sustained-hydrogen-evolution" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/138342.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">216</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">5</span> Increasing Photosynthetic H2 Production by in vivo Expression of Re-Engineered Ferredoxin-Hydrogenase Fusion Protein in the Green Alga Chlamydomonas reinhardtii</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Dake%20Xiong">Dake Xiong</a>, <a href="https://publications.waset.org/abstracts/search?q=Ben%20Hankamer"> Ben Hankamer</a>, <a href="https://publications.waset.org/abstracts/search?q=Ian%20Ross"> Ian Ross</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The most urgent challenge of our time is to replace the depleting resources of fossil fuels by sustainable environmentally friendly alternatives. Hydrogen is a promising CO2-neutral fuel for a more sustainable future especially when produced photo-biologically. Hydrogen can be photosynthetically produced in unicellular green alga like Chlamydomonas reinhardtii, catalysed by the inducible highly active and bidirectional [FeFe]-hydrogenase enzymes (HydA). However, evolutionary and physiological constraints severely restrict the hydrogen yield of algae for industrial scale-up, mainly due to its competition among other metabolic pathways on photosynthetic electrons. Among them, a major challenge to be resolved is the inferior competitiveness of hydrogen production (catalysed by HydA) with NADPH production (catalysed by ferredoxin-NADP+-reductase (FNR)), which is essential for cell growth and takes up ~95% of photosynthetic electrons. In this work, the in vivo hydrogen production efficiency of mutants with ferredoxin-hydrogenase (Fd*-HydA1*) fusion protein construct, where the electron donor ferredoxin (Fd*) is fused to HydA1* and expressed in the model organism C. reinhardtii was investigated. Once Fd*-HydA1* fusion gene is expressed in algal cells, the fusion enzyme is able to draw the redistributed photosynthetic electrons and use them for efficient hydrogen production. From preliminary data, mutants with Fd*-HydA1* transgene showed a ~2-fold increase in the photosynthetic hydrogen production rate compared with its parental strain, which only possesses the native HydA in vivo. Therefore, a solid method of having more efficient hydrogen production in microalgae can be achieved through the expression of the synthetic enzymes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Chlamydomonas%20reinhardtii" title="Chlamydomonas reinhardtii">Chlamydomonas reinhardtii</a>, <a href="https://publications.waset.org/abstracts/search?q=ferredoxin" title=" ferredoxin"> ferredoxin</a>, <a href="https://publications.waset.org/abstracts/search?q=fusion%20protein" title=" fusion protein"> fusion protein</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogen%20production" title=" hydrogen production"> hydrogen production</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogenase" title=" hydrogenase"> hydrogenase</a> </p> <a href="https://publications.waset.org/abstracts/86797/increasing-photosynthetic-h2-production-by-in-vivo-expression-of-re-engineered-ferredoxin-hydrogenase-fusion-protein-in-the-green-alga-chlamydomonas-reinhardtii" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/86797.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">262</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">4</span> The Effects of Varying Nutrient Conditions on Hydrogen Production in PGR5 Deficient C. Reinhardtii Mutants</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Samuel%20Mejorado">Samuel Mejorado</a> </p> <p class="card-text"><strong>Abstract:</strong></p> C. Reinahrdtii serves as one of the most promising organisms from which to obtain biological hydrogen. However, its production catalyst, [FeFe]-hydrogenase, is largely inhibited by the presence of oxygen. In recent years, researchers have identified a Proton Gradient Regulation 5 (PGR5) deficient mutant, which shows enhanced respiration and lower accumulations of oxygen within the system. In this research, we investigated the effects of varying nutrient conditions on PGR5 mutants' ability to produce hydrogen. After growing PGR5 mutants in varying nutrient conditions under 55W fluorescent lamps at 30℃ with constant stirring at 200 rpm, a common water displacement method was utilized to obtain a definitive volumetric reading of hydrogen produced by these mutants over a period of 12 days. After the trials, statistical t-tests and ANOVAs were performed to better determine the effect which nutrient conditions have on PGR5 mutants' ability to produce hydrogen. In this, we report that conditions of sulfur deprivation most optimally enhanced hydrogen production within these mutants, with groups grown under these conditions demonstrating the highest production capacity over the entire 12-day period. Similarly, it was found that when grown under conditions of nitrogen deprivation, a favorable shift towards carbon fixation and overall lipid/starch metabolism was observed. Overall, these results demonstrate that PGR5-deficient mutants stand as a promising source of biohydrogen when grown under conditions of sulfur deprivation. To date, photochemical characteristics of [FeFe]-hydrogenase in these mutants have yet to be investigated under conditions of sulfur deprivation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biofuel" title="biofuel">biofuel</a>, <a href="https://publications.waset.org/abstracts/search?q=biohydrogen" title=" biohydrogen"> biohydrogen</a>, <a href="https://publications.waset.org/abstracts/search?q=%5BFeFe%5D-hydrogenase" title=" [FeFe]-hydrogenase"> [FeFe]-hydrogenase</a>, <a href="https://publications.waset.org/abstracts/search?q=algal%20biofuel" title=" algal biofuel"> algal biofuel</a> </p> <a href="https://publications.waset.org/abstracts/160695/the-effects-of-varying-nutrient-conditions-on-hydrogen-production-in-pgr5-deficient-c-reinhardtii-mutants" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/160695.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">142</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">3</span> Algal/Bacterial Membrane Bioreactor for Bioremediation of Chemical Industrial Wastewater Containing 1,4 Dioxane</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ahmed%20Tawfik">Ahmed Tawfik</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Oxidation of 1,4 dioxane produces metabolites by-products involving glycolaldehyde and acids that have geno- and cytotoxicity impact on microbial degradation. Thereby, the incorporation of algae with bacteria in the treatment system would eliminate and overcome the accumulation of metabolites that are utilized as a carbon source for the build-up of biomass. Therefore, the aim of the present study is to assess the potential of algae/bacteria-based membrane bioreactor (AB-MBR) for biodegradation of 1,4 dioxane-rich wastewater at a high imposed loading rate. Three identical reactors, i.e., AB-MBR1, AB-MBR2, and AB-MBR3, were operated in parallel at 1,4 dioxane loading rates of 641.7, 320.9, and 160.4 mg/L. d., and HRTs of 6.0, 12 and 24 h. respectively. The AB-MBR1 achieved 1,4 dioxane removal rate of 263.7 mg/L.d., where the residual value in the treated effluent amounted to 94.4±22.9 mg/L. Reducing the 1,4 dioxane loading rate (LR) to 320.9 mg/L.d in the AB-MBR2 maximized the removal rate efficiency of 265.9 mg/L.d., with a removal efficiency of 82.8±3.2%. The minimum value of 1,4 dioxane of 17.3±1.8 mg/L in the treated effluent of AB-MBR3 was obtained at an HRT of 24.0 h and loading rate of 160.4 mg/L.d. The mechanism of 1,4 dioxane degradation in AB-MBR was a combination of volatilization (8.03±0.6%), UV oxidation (14.1±0.9%), microbial biodegradation (49.1±3.9%) and absorption/uptake and assimilation by algae (28.8±2.%). Further, the Thioclava, Afipia, and Mycobacterium genera oxidized and produced the required enzymes for hydrolysis and cleavage of the dioxane ring into 2-hydroxy-1,4 dioxane. Moreover, the fungi, i.e., Basidiomycota and Cryptomycota, played a big role in the degradation of the 1,4 dioxane into 2-hydroxy-1,4 dioxane. Xanthobacter and Mesorhizobium were involved in the metabolism process by secreting alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), and glycolate oxidase. Bacteria and fungi produced dehydrogenase (DH) for the transformation of 2-hydroxy-1,4 dioxane into 2-hydroxy-ethoxyacetaldehyde. The latter is converted into Ethylene glycol by Aldehyde hydrogenase (ALDH). Ethylene glycol is oxidized into acids using Alcohol hydrogenase (ADH). The Diatomea, Chlorophyta, and Streptophyta utilize the metabolites for biomass assimilation and produce the required oxygen for further oxidation of the dioxane and its metabolites by-products of bacteria and fungi. The major portion of metabolites (ethylene glycol, glycolic acid, and oxalic acid were removed due to uptake and absorption by algae (43±4.3%), followed by adsorption (18.4±0.9%). The volatilization and UV oxidation contribution for the degradation of metabolites were 8.7±0.7% and 12.3±0.8%, respectively. The capabilities of genera Defluviimonas, Thioclava, Luteolibacter, and Afipia. The genera of Defluviimonas, Thioclava, Luteolibacter, and Mycobacterium were grown under a high 1,4 dioxane LR of 641.7 mg/L.d. The Chlorophyta (4.1-43.6%), Streptophyta (2.5-21.7%), and Diatomea (0.8-1.4%) phyla were dominant for degradation of 1,4 dioxane. The results of this study strongly demonstrated that the bioremediation and bioaugmentation process can safely remove 1,4 dioxane from industrial wastewater while minimizing environmental concerns and reducing economic costs. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=wastewater" title="wastewater">wastewater</a>, <a href="https://publications.waset.org/abstracts/search?q=membrane%20bioreactor" title=" membrane bioreactor"> membrane bioreactor</a>, <a href="https://publications.waset.org/abstracts/search?q=bacterial%20community" title=" bacterial community"> bacterial community</a>, <a href="https://publications.waset.org/abstracts/search?q=algal%20community" title=" algal community"> algal community</a> </p> <a href="https://publications.waset.org/abstracts/183162/algalbacterial-membrane-bioreactor-for-bioremediation-of-chemical-industrial-wastewater-containing-14-dioxane" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/183162.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">43</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">2</span> Manganese Imidazole Complexes: Electrocatalytic Hydrogen Production</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Vishakha%20Kaim">Vishakha Kaim</a>, <a href="https://publications.waset.org/abstracts/search?q=Mookan%20Natarajan"> Mookan Natarajan</a>, <a href="https://publications.waset.org/abstracts/search?q=Sandeep%20Kaur-Ghumaan"> Sandeep Kaur-Ghumaan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Hydrogen is one of the most abundant elements present on earth’s crust and considered to be the simplest element in existence. It is not found naturally as a gas on earth and thus has to be manufactured. Hydrogen can be produced from a variety of sources, i.e., water, fossil fuels, or biomass and it is a byproduct of many chemical processes. It is also considered as a secondary source of energy commonly referred to as an energy carrier. Though hydrogen is not widely used as a fuel, it still has the potential for greater use in the future as a clean and renewable source of energy. Electrocatalysis is one of the important source for the production of hydrogen which could contribute to this prominent challenge. Metals such as platinum and palladium are considered efficient for hydrogen production but with limited applications. As a result, a wide variety of metal complexes with earth abundant elements and varied ligand environments have been explored for the electrochemical production of hydrogen. In nature, [FeFe] hydrogenase enzyme present in DesulfoVibrio desulfuricans and Clostridium pasteurianum catalyses the reversible interconversion of protons and electrons into dihydrogen. Since the first structure for the enzyme was reported in 1990s, a range of iron complexes has been synthesized as structural and functional mimics of the enzyme active site. Mn is one of the most desirable element for sustainable catalytic transformations, immediately behind Fe and Ti. Only limited number manganese complexes have been reported in the last two decades as catalysts for proton reduction. Furthermore, redox reactions could be carried out in a facile manner, due to the capability of manganese complexes to be stable at different oxidation states. Herein are reported, four µ2-thiolate bridged manganese complexes [Mn₂(CO)₆(μ-S₂N₄C₁₄H₁₀)] 1, [Mn₂(CO)7(μ- S₂N₄C₁₄H₁₀)] 2, Mn₂(CO)₆(μ-S₄N₂C₁₄H₁₀)] 3 and [Mn₂(CO)(μ- S₄N₂C₁₄H₁₀)] 4 have been synthesized and characterized. The cyclic voltammograms of the complexes displayed irreversible reduction peaks in the range - 0.9 to -1.3 V (vs. Fc⁺/Fc in acetonitrile at 0.1 Vs⁻¹). The complexes were catalytically active towards proton reduction in the presence of trifluoroacetic acid as seen from electrochemical investigations. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=earth%20abundant" title="earth abundant">earth abundant</a>, <a href="https://publications.waset.org/abstracts/search?q=electrocatalytic" title=" electrocatalytic"> electrocatalytic</a>, <a href="https://publications.waset.org/abstracts/search?q=hydrogen" title=" hydrogen"> hydrogen</a>, <a href="https://publications.waset.org/abstracts/search?q=manganese" title=" manganese"> manganese</a> </p> <a href="https://publications.waset.org/abstracts/80317/manganese-imidazole-complexes-electrocatalytic-hydrogen-production" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/80317.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">172</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">1</span> Effect of Non-Regulated pH on the Dynamics of Dark Fermentative Biohydrogen Production with Suspended and Immobilized Cell Culture </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Joelle%20Penniston">Joelle Penniston</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20B.%20Gueguim-Kana"> E. B. Gueguim-Kana </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Biohydrogen has been identified as a promising alternative to the use of non-renewable fossil reserves, owing to its sustainability and non-polluting nature. pH is considered as a key parameter in fermentative biohydrogen production processes, due to its effect on the hydrogenase activity, metabolic activity as well as substrate hydrolysis. The present study assesses the influence of regulating pH on dark fermentative biohydrogen production. Four experimental hydrogen production schemes were evaluated. Two were implemented using suspended cells under regulated pH growth conditions (Sus_R) and suspended and non-regulated pH (Sus_N). The two others regimes consisted of alginate immobilized cells under pH regulated growth conditions (Imm_R) and immobilized and non-pH regulated conditions (Imm_N). All experiments were carried out at 37.5°C with glucose as sole source of carbon. Sus_R showed a lag time of 5 hours and a peak hydrogen fraction of 36% and a glucose degradation of 37%, compared to Sus_N which showed a peak hydrogen fraction of 44% and complete glucose degradation. Both suspended culture systems showed a higher peak biohydrogen fraction compared to the immobilized cell system. Imm_R experiments showed a lag phase of 8 hours, a peak biohydrogen fraction of 35%, while Imm_N showed a lag phase of 5 hours, a peak biohydrogen fraction of 22%. 100% glucose degradation was observed in both pH regulated and non-regulated processes. This study showed that biohydrogen production in batch mode with suspended cells in a non-regulated pH environment results in a partial degradation of substrate, with lower yield. This scheme has been the culture mode of choice for most reported studies in biohydrogen research. The relatively lower slope in pH trend of the non-regulated pH experiment with immobilized cells (Imm_N) compared to Sus_N revealed that that immobilized systems have a better buffering capacity compared to suspended systems, which allows for the extended production of biohydrogen even under non-regulated pH conditions. However, alginate immobilized cultures in flask systems showed some drawbacks associated to high rate of gas production that leads to increased buoyancy of the immobilization beads. This ultimately impedes the release of gas out of the flask. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=biohydrogen" title="biohydrogen">biohydrogen</a>, <a href="https://publications.waset.org/abstracts/search?q=sustainability" title=" sustainability"> sustainability</a>, <a href="https://publications.waset.org/abstracts/search?q=suspended" title=" suspended"> suspended</a>, <a href="https://publications.waset.org/abstracts/search?q=immobilized" title=" immobilized "> immobilized </a> </p> <a href="https://publications.waset.org/abstracts/40020/effect-of-non-regulated-ph-on-the-dynamics-of-dark-fermentative-biohydrogen-production-with-suspended-and-immobilized-cell-culture" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40020.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">342</span> </span> </div> </div> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Explore <li><a href="https://waset.org/disciplines">Disciplines</a></li> <li><a href="https://waset.org/conferences">Conferences</a></li> <li><a href="https://waset.org/conference-programs">Conference Program</a></li> <li><a href="https://waset.org/committees">Committees</a></li> <li><a href="https://publications.waset.org">Publications</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Research <li><a href="https://publications.waset.org/abstracts">Abstracts</a></li> <li><a href="https://publications.waset.org">Periodicals</a></li> <li><a href="https://publications.waset.org/archive">Archive</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Open Science <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Philosophy.pdf">Open Science Philosophy</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Award.pdf">Open Science Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Society-Open-Science-and-Open-Innovation.pdf">Open Innovation</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Postdoctoral-Fellowship-Award.pdf">Postdoctoral Fellowship Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Scholarly-Research-Review.pdf">Scholarly Research Review</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Support <li><a href="https://waset.org/page/support">Support</a></li> <li><a href="https://waset.org/profile/messages/create">Contact Us</a></li> <li><a href="https://waset.org/profile/messages/create">Report Abuse</a></li> </ul> </div> </div> </div> </div> </div> <div class="container text-center"> <hr style="margin-top:0;margin-bottom:.3rem;"> <a href="https://creativecommons.org/licenses/by/4.0/" target="_blank" class="text-muted small">Creative Commons Attribution 4.0 International License</a> <div id="copy" class="mt-2">© 2024 World Academy of Science, Engineering and Technology</div> </div> </footer> <a href="javascript:" id="return-to-top"><i class="fas fa-arrow-up"></i></a> <div class="modal" id="modal-template"> <div class="modal-dialog"> <div class="modal-content"> <div class="row m-0 mt-1"> <div class="col-md-12"> <button type="button" class="close" data-dismiss="modal" aria-label="Close"><span aria-hidden="true">×</span></button> </div> </div> <div class="modal-body"></div> </div> </div> </div> <script src="https://cdn.waset.org/static/plugins/jquery-3.3.1.min.js"></script> <script src="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/js/bootstrap.bundle.min.js"></script> <script src="https://cdn.waset.org/static/js/site.js?v=150220211556"></script> <script> jQuery(document).ready(function() { /*jQuery.get("https://publications.waset.org/xhr/user-menu", function (response) { jQuery('#mainNavMenu').append(response); });*/ jQuery.get({ url: "https://publications.waset.org/xhr/user-menu", cache: false }).then(function(response){ jQuery('#mainNavMenu').append(response); }); }); </script> </body> </html>