Refine
Year of publication
Institute
- Fachbereich Medizintechnik und Technomathematik (1565)
- Fachbereich Elektrotechnik und Informationstechnik (711)
- IfB - Institut für Bioengineering (564)
- Fachbereich Energietechnik (561)
- Fachbereich Chemie und Biotechnologie (537)
- INB - Institut für Nano- und Biotechnologien (533)
- Fachbereich Luft- und Raumfahrttechnik (481)
- Fachbereich Maschinenbau und Mechatronik (262)
- Fachbereich Wirtschaftswissenschaften (205)
- Solar-Institut Jülich (161)
Has Fulltext
- no (4686) (remove)
Language
- English (4686) (remove)
Document Type
- Article (3194)
- Conference Proceeding (1033)
- Part of a Book (191)
- Book (144)
- Doctoral Thesis (30)
- Conference: Meeting Abstract (28)
- Patent (25)
- Other (10)
- Report (9)
- Conference Poster (5)
Keywords
- Gamification (6)
- avalanche (6)
- Earthquake (5)
- Enterprise Architecture (5)
- MINLP (5)
- solar sail (5)
- Additive manufacturing (4)
- Diversity Management (4)
- Energy storage (4)
- Engineering optimization (4)
Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 Å as well as in complex with CoA at a resolution of 1.59 Å. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called “hot dog fold” which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all “hot dog fold” proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041–2053. © 2014 Wiley Periodicals, Inc.
In this work, the catalyst manganese(IV) oxide (MnO2), of calorimetric gas sensors (to monitor the sterilization agent vaporized hydrogen peroxide) has been investigated in more detail. Chemical analyses by means of X-ray-induced photoelectron spectroscopy have been performed to unravel the surface chemistry prior and after exposure to hydrogen peroxide vapor at elevated temperature, as applied in the sterilization processes of beverage cartons. The surface characterization reveals a change in oxidation states of the metal oxide catalyst after exposure to hydrogen peroxide. Additionally, a cleaning effect of the catalyst, which itself is attached to the sensor surface by means of a polymer interlayer, could be observed.
The Dry Low NOx (DLN) Micromix combustion principle with increased energy density is adapted for the industrial gas turbine APU GTCP 36-300 using hydrogen and hydrogen-rich syngas with a composition of 90%-Vol. hydrogen (H₂) and 10%-Vol. carbon-monoxide (CO). Experimental and numerical studies of several combustor geometries for hydrogen and syngas show the successful advance of the DLN Micromix combustion from pure hydrogen to hydrogen-rich syngas. The impact of the different fuel properties on the combustion principle and aerodynamic flame stabilization design laws, flow field, flame structure and emission characteristics is investigated by numerical analysis using a hybrid Eddy Break Up combustion model and validated against experimental results.