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Optical control of enzymatic activity. Light is an important signal for inducing and regulating chemical reactions because it is orthogonal to other mechanisms of functional control such as small-molecule binding or protein-protein interaction, and it is applicable with high spatial and temporal precision. In nature, light is absorbed by photosensory domains which transmit the incoming signal via structural (steric, dynamic, or electronic) changes to a tethered protein. Several classes of photosensory proteins exist which differ with respect to photochemisry,  chromophor and thus, absorbed light energy. Light-oxygen voltage (LOV) domains are among the best studied photoreceptors that are linked to effector domains such as kinases, phosphodiesterases, or DNA-binding proteins.

© AK-Brakmann​/​TU Dortmund
Figure 1. (A) Structure of a typical LOV domain (here: Avena sativa phototropin-1, AsLOV2, dark state; PDB: 2v1a). (B) Schematic depiction of the LOV domain’s photocycle. (Figure directly reproduced from: S. Seifert and S. Brakmann, ACS Chem. Biol. 13 (2018), 1914-1920.)

We are investigating how LOV domains can be combined with enzymes which are not naturally regulated by light. A recent example concerns nucleic acid polymerases, the core proteins that mediate replication of DNA and RNA in all types of cells. Our research aims at understanding mechanisms of allosteric protein switching even in proteins with complex catalytic activity and at generating tools for studying the roles of these enzymes in cellular, developmental and disease-related processes.

© AK-Brakmann​/​TU Dortmund
Figure 2. Structures of bacteriophage T7 RNA polymerase (A) in its initiation complex (IC, PDB: 2pi4), and (B) in its elongation state (EC, PDB: 1h38), with positions of LOV domain insertion marked by blue spheres. (Figure directly reproduced from: S. Seifert et al., ChemBioChem 2019 Jun 13. doi: 10.1002/cbic.201900298. [Epub ahead of print].)


Enzymatic reaction cascades. Enzymes are very efficient catalysts and ideally suited for application in a sustainable chemistry because they typically accelerate reactions by factors of 108-1010, are applied at low mole percentage (10-3-10-4), are environmentally benign (completely biodegradable), act under mild conditions, and neither are restricted to their natural role nor to their natural substrate.

We are, for example, currently investigating whether the simple reaction

could be forced towards the production and utilization of carbonate using enzymatic catalysis. In the simplest case, carbonate could be precipitated but it may also be employed as a substrate in organic synthesis. Candidate enzymes for this reaction scheme include carbonic anhydrases as well as enzymes for the turnover of bicarbonate.

© AK-Brakmann​/​TU Dortmund

Location & approach

The campus of TU Dort­mund University is located close to interstate junction Dort­mund West, where the Sauerlandlinie A 45 (Frankfurt-Dort­mund) crosses the Ruhrschnellweg B 1 / A 40. The best interstate exit to take from A 45 is "Dort­mund-Eichlinghofen" (closer to Campus Süd), and from B 1 / A 40 "Dort­mund-Dorstfeld" (closer to Campus Nord). Signs for the uni­ver­si­ty are located at both exits. Also, there is a new exit before you pass over the B 1-bridge leading into Dort­mund.

To get from Campus Nord to Campus Süd by car, there is the connection via Vogelpothsweg/Baroper Straße. We recommend you leave your car on one of the parking lots at Campus Nord and use the H-Bahn (suspended monorail system), which conveniently connects the two campuses.

TU Dort­mund University has its own train station ("Dort­mund Uni­ver­si­tät"). From there, suburban trains (S-Bahn) leave for Dort­mund main station ("Dort­mund Hauptbahnhof") and Düsseldorf main station via the "Düsseldorf Airport Train Station" (take S-Bahn number 1, which leaves every 20 or 30 minutes). The uni­ver­si­ty is easily reached from Bochum, Essen, Mülheim an der Ruhr and Duisburg.

You can also take the bus or subway train from Dort­mund city to the uni­ver­si­ty: From Dort­mund main station, you can take any train bound for the Station "Stadtgarten", usually lines U41, U45, U 47 and U49. At "Stadtgarten" you switch trains and get on line U42 towards "Hombruch". Look out for the Station "An der Palmweide". From the bus stop just across the road, busses bound for TU Dort­mund University leave every ten minutes (445, 447 and 462). Another option is to take the subway routes U41, U45, U47 and U49 from Dort­mund main station to the stop "Dort­mund Kampstraße". From there, take U43 or U44 to the stop "Dort­mund Wittener Straße". Switch to bus line 447 and get off at "Dort­mund Uni­ver­si­tät S".

The H-Bahn is one of the hallmarks of TU Dort­mund University. There are two stations on Campus Nord. One ("Dort­mund Uni­ver­si­tät S") is directly located at the suburban train stop, which connects the uni­ver­si­ty directly with the city of Dort­mund and the rest of the Ruhr Area. Also from this station, there are connections to the "Technologiepark" and (via Campus Süd) Eichlinghofen. The other station is located at the dining hall at Campus Nord and offers a direct connection to Campus Süd every five minutes.

The AirportExpress is a fast and convenient means of transport from Dortmund Airport (DTM) to Dortmund Central Station, taking you there in little more than 20 minutes. From Dortmund Central Station, you can continue to the university campus by interurban railway (S-Bahn). A larger range of international flight connections is offered at Düsseldorf Airport (DUS), which is about 60 kilometres away and can be directly reached by S-Bahn from the university station.

The facilities of TU Dortmund University are spread over two campuses, the larger Campus North and the smaller Campus South. Additionally, some areas of the university are located in the adjacent "Technologiepark".

Site Map of TU Dortmund University (Second Page in English).