Register Now

May 16, 2024

CRC 1333 Minisymposium on "Catalysis under Confinement"

REGISTER NOW – May 16, 2024

Minisymposium "Catalysis under Confinement"

CRC Colloquium – Prof. Serena de Beer

2:00 pm – 3:00 pm

via WebEx video conference
CRC 1333
Please find Webex Link below!

We are very happy to welcome within the CRC 1333 Colloquium Series:

Prof. Serena de Beer
Department Inorganic Spectroscopy
Max Planck Institute for Chemical Energy Conversion

Thursday, January 13, 2022, 2:00 – 3:00 pm

Topic: The Evolution of Electronic Complexity in Biology: Advanced X-ray Spectroscopic Studies of Iron Sulfur Clusters

 via WebEx video conference

Meeting Link:

Meeting-ID: 2733 444 7596
Kenncode: riQZMdQn422

Her Research Activities:

  • Development and application of advanced X-ray spectroscopic tools for understanding processes in biological and chemical catalysis, namely:
    • Valence XES
    • Resonant Valence XES
    • 2p3d RIXS
  • Application of those and other  X-ray spectroscopic methods to investigate the following reactions catalyzed by earth-abundant metals
    • N2 reduction
    • CH4 oxidation
    • H2O oxidation
    • H2 production

The CRC cordially invites all who are interested to the lecture!


Iron sulfur proteins are ubiquitous in nature, performing essential roles in electron transfer processes, redox chemistry, regulatory sensing and catalysis. The metal active sites of these proteins range from simple single iron sites to complex eight iron clusters. Perhaps the most complex iron sulfur cluster that has been identified to date is the iron molybdenum cofactor (or FeMoco) of nitrogenase, which is capable of cleaving the strong triple bond of dinitrogen. The fundamental question that arises is how does nature evolve complexity in order to enable challenging transformations? In our view, a deeper understanding of the complex geometric and electronic structure of iron sulfur clusters requires the pursuit of novel experimental approaches for integrating their electronic structure in a detailed and quantitative fashion. To this end, we are applying both 2p3d and 1s3p resonant inelastic X-ray scattering (2p3d RIXS), in order to obtain deeper insights into the electronic structure of these important clusters. These data provide an experimental measure of the d-d transitions and allow for more detailed insights into the nature of the multiplet structure. The utility of these methods for understanding the electronic structure of nitrogenase will be highlighted. The challenges that RIXS spectroscopy presents for theoretical modeling will also be discussed.