TY  - JOUR
A1  - Heine, A.
A1  - Herrmann, G.
A1  - Selmer, Thorsten
A1  - Terwesten, F.
A1  - Buckel, W.
A1  - Reuter, K.
T1  - High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily
JF  - Proteins
N2  - 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.
Y1  - 2014
U6  - https://doi.org/10.1002/prot.24557
SN  - 1097-0134 (E-Journal); 0887-3585 (Print)
VL  - 82
IS  - 9
SP  - 2041
EP  - 2053
PB  - Wiley-Liss
CY  - New York
ER  - 
TY  - JOUR
A1  - Takenaga, Shoko
A1  - Biselli, Manfred
A1  - Schnitzler, Thomas
A1  - Öhlschläger, Peter
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
T1  - Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis–Menten-like kinetics for cell culturing
JF  - Physica status solidi A : Applications and materials science
N2  - The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17–200 mM) follows a Michaelis–Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.
Y1  - 2014
U6  - https://doi.org/10.1002/pssa.201330464
SN  - 1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)
VL  - 211
IS  - 6
SP  - 1410
EP  - 1415
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Guo, Yuanyuan
A1  - Miyamoto, Ko-ichiro
A1  - Wagner, Torsten
A1  - Schöning, Michael Josef
A1  - Yoshinobu, Tatsuo
T1  - Theoretical study and simulation of light-addressable potentiometric sensors
JF  - Physica status solidi (A) : applications and materials
N2  - The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.
Y1  - 2014
U6  - https://doi.org/10.1002/pssa.201330354
SN  - 0031-8965
VL  - 211
IS  - 6
SP  - 1467
EP  - 1472
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Whitehead, Mark
A1  - Öhlschläger, Peter
A1  - Almajhdi, Fahad N.
A1  - Alloza, Leonor
A1  - Marzábal, Pablo
A1  - Meyers, Ann E.
A1  - Hitzeroth, Inga I.
A1  - Rybicki, Edward P.
T1  - Human papillomavirus (HPV) type 16 E7 protein bodies cause tumour regression in mice
JF  - BMC cancer
Y1  - 2014
U6  - https://doi.org/10.1186/1471-2407-14-367
SN  - 1471-2407
IS  - 14:367
SP  - 1
EP  - 15
PB  - BioMed Central
CY  - London
ER  - 
TY  - JOUR
A1  - Raue, Markus
A1  - Wambach, M.
A1  - Glöggler, S.
A1  - Grefen, Dana
A1  - Kaufmann, R.
A1  - Abetz, C.
A1  - Georgopanos, P.
A1  - Handge, U. A.
A1  - Mang, Thomas
A1  - Blümich, B.
A1  - Abetz, V.
T1  - Investigation of historical hard rubber ornaments of Charles Goodyear
JF  - Macromolecular chemistry and physics
Y1  - 2014
SN  - 1022-1352
VL  - Vol. 215
IS  - No. 3
SP  - 245
EP  - 254
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Nachtrodt, Frederik
A1  - Tietsch, Wolfgang
A1  - Mostacci, Domiziano
A1  - Scherer, Ulrich W.
T1  - Set-up and first operation of a plasma oven for treatment of low level radioactive wastes
JF  - Nuclear technology and radiation protection
Y1  - 2014
U6  - https://doi.org/10.2298/NTRP140SS47N
SN  - 1451-3994
VL  - 29
IS  - Suppl.
SP  - 47
EP  - 51
PB  - VINČA Institute of Nuclear Sciences
CY  - Belgrad
ER  - 
TY  - JOUR
A1  - Ratke, Lorenz
A1  - Milow, Barbara
A1  - Lisinski, Susanne
A1  - Hoepfner, Sandra
T1  - On an effect of fine ceramic particles on the structure of aerogels
JF  - Microgravity science and technology
Y1  - 2014
U6  - https://doi.org/10.1007/s12217-014-9380-2
SN  - 0938-0108 ; 1875-0494
VL  - 26
SP  - 103
EP  - 110
PB  - Springer Nature
CY  - Heidelberg
ER  - 
TY  - GEN
A1  - Tippkötter, Nils
A1  - Sieker, T.
A1  - Wiesen, S.
A1  - Duwe, A.
A1  - Roth, J.
A1  - Ulber, Roland
T1  - Simultane Saccharifizierung und Fermentierung (SSF) sowie Produktion von Aceton, Butanol, Ethanol (ABE) und Dicarbonsäuren aus technischer Cellulose
T2  - Chemie Ingenieur Technik
N2  - Technische Cellulose wurde als möglicher Rohstoff zur fermentativen Produktbildung untersucht. Hierfür wird Cellulose in der Lignocellulose-Bioraffinerie hergestellt und daraus Hydrolysat gewonnen. Die Prüfung der technischen Hydrolysate als Substrate erfolgte anhand eines breiten Spektrums an Bioprodukten, von Kraftstoffen wie Ethanolund Butanol, bis zu den Dicarbonsäuren Itacon- und Bernsteinsäure. Dabei werden Bakterien, Hefen und Pilze als Produktionsorganismen eingesetzt. Die einzelnen Herstellverfahren stellen unterschiedliche Anforderungen an die Substrathandhabung. Im Fall der Ethanol- und Butanol-Gewinnung kann eine simultane Saccharifizierung und Fermentierung (SSF) durchgeführt werden. Aufgrund der Produkttoxizität erfordert die Butanol-Herstellung dabei eine In-situ-Produktabtrennung durch Lösemittelimprägnierte Partikel. Die Herstellung der beiden Dicarbonsäuren unterscheidet sich in der Sensitivität der verwendeten Mikroorganismen gegenüber Inhibitoren, die in Spuren im Hydrolysat enthalten sind. Die Bernteinsäurebildung mit Actinobacillussuccinogenes kann mit unbehandeltem Hydrolysat erfolgen. Dagegen erfordert die Gewinnung von Itaconsäure mit A. terreus eine Detoxifizierung des Hydrolysats. Insgesamt konnte gezeigt werden, dass sämtliche Bioraffinerie-Hydrolysate als Substrate für unterschiedliche Fermentationen geeignet sind.
Y1  - 2014
U6  - https://doi.org/10.1002/cite.201450297
SN  - 0009-286X
SN  - 1522-2640 (eISSN)
N1  - ProcessNet-Jahrestagung 2014 und 31. DECHEMA-Jahrestagung der Biotechnologen, 30. September - 2. Oktober 2014, Eurogress Aachen
VL  - 86
IS  - 9
SP  - 1518
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Handtke, Stefan
A1  - Schroeter, Rebecca
A1  - Jürgen, Britta
A1  - Methling, Karen
A1  - Schlüter, Rabea
A1  - Albrecht, Dirk
A1  - Hijum, Sacha A. F. T. van
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Lalk, Michael
A1  - Schweder, Thomas
A1  - Hecker, Michael
A1  - Voigt, Birgit
T1  - Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress
JF  - PLOS one
N2  - Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.
Y1  - 2014
U6  - https://doi.org/10.1371/journal.pone.0085625
SN  - 1932-6203
VL  - 9
IS  - 1
PB  - PLOS
CY  - San Francisco
ER  - 
TY  - JOUR
A1  - Küppers, Tobias
A1  - Steffen, Victoria
A1  - Hellmuth, Hendrik
A1  - O'Connell, Timothy
A1  - Bongaerts, Johannes
A1  - Maurer, Karl-Heinz
A1  - Wiechert, Wolfgang
T1  - Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer
JF  - Microbial cell factories
Y1  - 2014
U6  - https://doi.org/10.1186/1475-2859-13-46
SN  - 1475-2859 (E-Journal)
VL  - 13
SP  - Article No. 46
PB  - BioMed Central
CY  - London
ER  -