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Dr Hyeryeong Lee

UKRI Research Fellow

I am currently working on development of a semi-artificial photosynthetic system powered by cyanobacteria, under the supervision of Dr. Jenny Zhang at the University of Cambridge. My research focuses on genetically engineering protein topologies within cyanobacterial cells to enhance their light-harvesting capability and bioenergy production. Prior to this, I earned my M.S. (2017) and Ph.D. (2022) degrees from the Gwangju Institute of Science and Technology, where I was honored with the Graduate Research Excellence Award, achieving 1st place upon Ph.D. graduation. My doctoral research centered on utilizing protein-engineering approaches to control the orientation of (multi-)enzymes on electrode surfaces, thereby enhancing enzymatic chain reaction rates and improving electrical communication at the enzyme-electrode interfaces. My academic journey has been supported by prestigious fellowships, including the Global Ph.D. Fellowship (GPF) and the Basic Science Research Fellowship, both funded by the National Research Foundation of Korea. Additionally, I was once selected as one of 15 nationwide representatives for the 9th Global Young Scientist Summit (GYSS) in Singapore, an opportunity that broadened my scientific perspective and network. In 2024, I joined the University of Cambridge after being awarded the Marie Curie Fellowship, expanding my expertise from protein-based electrochemistry to photosynthetic microbe-based "photobioelectrochemistry." My current research interests lie in biophotovoltaics, synthetic biology, cyanobacterial and protein engineering, photosystem modifications, and (photo)bioelectrochemistry.

Publications

Wire-ready invertase-glucose dehydrogenase chimera as a strategic design for enzymatic chain reaction-driven electrocatalysis
H Lee, Y Bang, JS Sravan, B Kang, IS Chang
– Electrochimica Acta
(2025)
509,
145283
(doi: 10.1016/j.electacta.2024.145283)
A Redox-Enzyme Integrated Microbial Fuel Cell Design Using the Surface Display System in Shewanella oneidensis MR-1.
S Baek, H Lee, YS Lee, IS Chang, I-G Choi
– ACS Applied Materials & Interfaces
(2024)
17,
1167
(doi: 10.1021/acsami.4c16868)
Advanced strategies for enzyme–electrode interfacing in bioelectrocatalytic systems
H Lee, SS Reginald, JS Sravan, M Lee, IS Chang
– Trends in biotechnology
(2024)
S0167-7799(24)00344-5
(doi: 10.1016/j.tibtech.2024.11.015)
NADH-dependent CO2 reductase on graphite for capacitive electrocatalytic interfacing mediated by solid-binding peptide.
J Shanthi Sravan, H Lee, Y Bang, IS Chang
– Bioresour Technol
(2024)
417,
131841
(doi: 10.1016/j.biortech.2024.131841)
Orientation-Controllable Enzyme Cascade on Electrode for Bioelectrocatalytic Chain Reaction.
H Lee, Y Bang, IS Chang
– ACS Applied Materials & Interfaces
(2023)
15,
40355
(doi: 10.1021/acsami.3c03077)
Regulatory transcription factor (CooA)-driven carbon monoxide partial pressure sensing whole-cell biosensor
B Kang, H Lee, S Oh, J-Y Kim, Y-J Ko, IS Chang
– Heliyon
(2023)
9,
e17391
(doi: 10.1016/j.heliyon.2023.e17391)
Versatile Biosynthetic Approach to Regioselective Enzyme Patterning for Direct Bioelectrocatalysis Application
H Lee, SS Reginald, IS Chang
– Advanced Materials Technologies
(2023)
8,
(doi: 10.1002/admt.202201324)
Direct electrical contact of NAD+/NADH-dependent dehydrogenase on electrode surface enabled by non-native solid-binding peptide as a molecular binder
SS Reginald, MJ Kim, H Lee, N Fazil, S Choi, S Oh, J Seo, IS Chang
– Electrochimica Acta
(2022)
421,
140480
(doi: 10.1016/j.electacta.2022.140480)
Protocol for construction and characterization of direct electron transfer-based enzyme-electrode using gold binding peptide as molecular binder
H Lee, EM Lee, SS Reginald, IS Chang
– STAR Protocols
(2022)
3,
101466
(doi: 10.1016/j.xpro.2022.101466)
Control of carbon monoxide dehydrogenase orientation by site-specific immobilization enables direct electrical contact between enzyme cofactor and solid surface
SS Reginald, H Lee, N Fazil, B Sharif, M Lee, MJ Kim, H Beyenal, IS Chang
– Commun Biol
(2022)
5,
390
(doi: 10.1038/s42003-022-03335-7)
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01223 763137

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