Ms. Katrina Hong

Photo of Katrina  Hong

Katrina Hong M.Sc.

Max-Planck-Institute for Chemical Energy Conversion
Group Lubitz, Biophysical Chemistry Department
Max-Planck-Institute for Chemical Energy Conversion
Stiftstrasse 34 - 36
Building: Sonderbau
Floor/Room: EG.345
45470 Muelheim an der Ruhr
Phone +49 208 306 - 3845

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • B.Sc. 2011, University of California, Berkeley, USA

Second degree and/or intermediate examination:

  • M.Sc. 2012, Heinrich-Heine University, Duesseldorf, Germany


  • Dean‘s List (2008, 2010, 2011, University of California, Berkeley)
  • Berkeley Scholarship (2010 - 2011, University of California, Berkeley)
  • Cal Alumni Leadership Award (2010 - 2011, University of California, Berkeley)
  • HCC Awarded and Paid Intern at Lucile Packard Children‘s Hospital at Stanford (2011)

BioStruct PhD project

Rapid Time Scale Determination of Substrate Binding Kinetics for Biological Metallocofactors.
The development of synthetic catalysts for a diverse number of chemical problems is increasingly turning to nature for inspiration as biological systems use cheap, abundant materials, such as manganese and iron complexes, to do complex multi-electron chemistry. The variety of reactions they perform includes: a) radical scavenging in biological systems; b) energy production and storage; and c) biosynthesis and cellular repair, to name but three. Rapid time scale determination of substrate binding kinetics for biological metallocofactors is important in understanding the chemistry these complexes perform and to resolve, in detail, the interaction of the substrate with the cofactor. In multi-electron-reactions such as water-splitting, the catalyst must cycle through several different oxidation states, many of which are paramagnetic. As such, EPR spectroscopy with its related pulse techniques is an invaluable tool for the elucidation of the properties of these cofactors. The BioStruct Doctoral Fellow is involved in the development of both spectroscopic and sample preparation methods for the trapping of biological reaction intermediates, for spectroscopic characterization. This entails isotopic labeling and the isolation of the various resting states of enzyme systems studied as well as redox poising and intermediate trapping using rapid freeze quench. Multi-frequency EPR spectroscopy will be the primary technique used in conjunction with FTIR, UV-VIS, Mossbauer, MCD, Resonance Raman and solid state NMR. Specific biological systems of interest include: i) HydG, a radical S-adenosylmethionine (SAM) enzyme involved in the maturation of the [FeFe] hydrogenase, it synthesizes CO and CN ligands as well as the bridging dithiolate of the iron cofactor; ii) the di-manganese catalase, which catalyzes the dismutation of H2O2 to H2O and O2; iii) a tetra-manganese oxygen evolving complex (OEC) of Photosystem II, which performs the multi-step oxidation of H2O to O2 and iii) the class I ribonucleotide reductase, which synthesizes all four DNA monomers and related systems.


Topic Supervisor:
undefinedProf. Dr. Wolfgang Lubitz, Institute for Biochemistry, Lubitz Group
Complementary Supervisor:
undefinedProf. Dr. Lutz Schmitt, Institute for Biochemistry, Schmitt Group
Third Supervisor:
Dr. Nicholas Cox

Responsible for the content: E-MailBioStruct Office