Dr Hanna Kwon

Supervisor Details

Contact Details

Department of Molecular and Cell Biology, University of Leicester

Scientific Background

Research Interests

Metalloenzyme mechanisms

In the 20th century, X-ray crystallography revealed a molecular world at a level previously unimaginable, far beyond the limits of the microscope. In my research group, we use structural biology techniques including but not limited to X-ray and neutron crystallography, and X-ray free electron laser to understand the mechanisms of metalloenzymes. X-ray crystallography is a powerful tool that gives three dimensional structures at atomic resolution; however, it only provides static pictures. Enzyme reactions are dynamic processes that take place in ultrafast time scale, necessitating the development of new tools and techniques to observe them.

The ultimate goal is to routinely produce “a molecular movie” through time-resolved crystallography utilising rapidly evolving synchrotrons, XFELs and cryoEM to better understand the structural dynamics of biomolecular catalysis.

One of our main research focuses is to understand the catalytic activity and biological function in heme proteins. Heme is essential for the survival of virtually all living systems and has long been recognised as the prosthetic group of the active site in proteins which play significant roles in catalysis, oxygen transport and electron transfer. These are some of life’s most fundamental processes. Our work on heme peroxidases is in collaboration with Professors Peter Moody (University of Leicester), Emma Raven (University of Bristol) and Dr Jon Warrall (University of Essex).

We also utilise neutron crystallography which has the unique power to visualise hydrogen atoms; essential in studying enzyme mechanisms. We collaborate with scientists at Institut Langevin in Grenoble, France and MLZ in Munich, Germany.

Supervision Style

In three words or phrases: Supportive, collaborative and student-driven.

Provision of Training

At the beginning of the project, I enjoy working with the student to develop appropriate methods and techniques. This way, I can provide training and we can formulate a research strategy together. Afterwards, I believe that PhD students should demonstrate a level of independence and lead the project.

Progression Monitoring and Management

We will meet regularly to discuss the progress of the project. We can identify and discuss challenges you may be experiencing. You will have ownership of the project and be responsible for planning day to day activities and I will provide guidance when necessary.

Communication

I have open door policy and will be available for discussions. PhD Students can expect scheduled meetings with me:

In a group meeting

At least once per fortnight

In year 1 of PhD study

At least once per fortnight

In year 2 of PhD study

At least once per fortnight

In year 3 of PhD study

At least once per fortnight

These meetings will be a mixture of face to face, via video chat or telephone, and although I have an open door policy my pattern of being contactable for an instant response is not predictable.

Work Pattern

The timing of work in my lab is completely flexible, and (other than attending pre-arranged meetings), I expect students to manage their own time.

Certain tasks in my lab need to occur at set times, and students need to be able to commit to a rota/timetable shared with other members of the team.

Notice Period for Feedback

I need at least 1 week’s notice to provide feedback on written work of up to 5000 words.

MIBTP Project Details

Current Projects (2025-26)

Primary supervisor for:

Unravelling the Mechanisms of Heme Delivery and Its Role in Cancer Biology

See the PhD Opportunities section to see if this project is currently open for applications via MIBTP.

Please Note: The main page lists projects via BBSRC Research Theme(s) quoted and then relevant Topic(s).

Unravelling the Mechanisms of Heme Delivery and Its Role in Cancer Biology

Secondary Supervisor(s): Professor Andrew Hudson

University of Registration: University of Leicester

BBSRC Research Themes: Understanding the Rules of Life (Structural Biology)

Project Outline

Heme is a vital small molecule involved in the function of numerous proteins. It plays key roles, such as binding oxygen in globins and facilitating electron transfer in cytochromes. Heme is synthesised in the mitochondria, however, we do not know the mechanism by which heme is transported to various cell compartments where it can be incorporated into different proteins. Since free heme is toxic, chaperone proteins that weakly bind and transport heme are essential for this process. Recently, a number of chaperone proteins, such as GAPDH, FLVCR1b, PGRMC1/2, etc., have been identified as important players in the heme delivery system, but the detailed molecular mechanisms behind heme transport pathways remains unclear.

In this PhD project, you will explore the mechanisms of intracellular heme delivery, focusing on how heme chaperones regulate the homeostasis of enzymes that are often overexpressed in cancer cells, namely the heme dioxygenases. Key questions include whether the suspected heme chaperones (named above) play a general role in intracellular heme delivery to dioxygenases, how they mediate heme binding and transfer, and how their interaction properties influence cellular heme transport.

You will:

Measure the heme-binding properties of wild-type and mutant heme chaperone proteins using isothermal calorimetry and UV-visible spectroscopy.
Evaluate the interaction of these chaperones with apo-heme dioxygenases and their ability to transfer heme using novel fluorescence techniques developed in the Kwon/Hudson laboratories.
Solve the structures of heme chaperone complexes and their interactions with the dioxygenases using cryo-electron microscopy (cryoEM), X-ray crystallography, and complementary spectroscopy techniques.

This project offers an exciting opportunity to deepen our understanding of a fundamental cellular process and its implications for cancer biology. The insights gained will not only shed light on the regulation and activation of heme dioxygenases but could also lead to novel therapeutic strategies for cancer and other diseases.

As a PhD student, you will gain a diverse set of interdisciplinary skills spanning structural biology, chemical biology, and biophysics.

Techniques

Techniques that will be undertaken during the project:

Molecular Biology (cloning & mutagenesis).
Protein expression and purification.
Enzyme kinetics.
Confocal and fluorescent microscopy.
Protein crystallisation.
Structure determination (X-ray crystallography & cryo-EM).

Previous Projects (2024-25)

Primary supervisor for:

Revealing Reactivity in Cancer-Associated Heme Proteins: Novel Time-Resolved Structural Approaches

Co-supervisor on a project with Dr Philip Ash.

Previous Projects (2023-24)

Primary supervisor for:

Control mechanisms of IDO1 in cancer cells