Zhu-Lin (Sam) Xie, Ph.D.

 

Biography

Zhu-Lin (Sam) Xie (pronunciation: zu lin sheh) joined the faculty in the Department of Chemistry and Biochemistry at FAU in the fall of 2023. Prior to joining FAU, he worked as a postdoctoral researcher at Argonne National Laboratory under the supervision of Dr. Karen Mulfort from 2019 to 2023, spearheading multiple projects encompassing solar energy conversion, electrochemical CO₂ reduction and synchrotron X-ray spectroscopy. Dr. Xie completed his graduate training at the University of Texas at Austin from 2013 to 2019 in the laboratory of Prof. Michael Rose. His doctoral research centered on developing synthetic models of [Fe]-hydrogenase. Before UT Austin, he earned a B.S. in chemistry from the University of Jinan in China in 2012.

Research Interests

The research interests within the Xie group encompass a wide range of areas at the intersection of synthetic inorganic chemistry, bioinorganic chemistry, catalysis, materials chemistry, and medicinal chemistry. In the current phase of our research, we are actively pursuing three key directions:

1. Molecular Electro- and Photocatalytic Systems for Energy Conversion: Our primary focus in this project is the development of molecular transition metal complexes that can catalyze crucial photo-driven or electro-driven energy-converting reactions. These include CO₂ reduction, H₂ evolution, and water oxidation. We are particularly interested in the exploration of bimetallic molecular electro- and photocatalytic systems to perform CO₂ reduction reaction. By harnessing the synergistic effects between metal centers, we aim to fine-tune catalysis and produce products beyond two-electron reduction. This research will provide valuable design principles for the development of catalytic systems for renewable energy production.
2. Artificial Enzymes for Catalysis: In this project, our objective is to design and synthesize molecular cages decorated with diverse functional groups, catalytic centers, and hydrogen bonding networks. These molecular cages, which we term "artificial enzymes", aim to mimic the functionalities of natural enzymes. By offering a confined space similar to that found in natural enzymes, they protect reaction centers, enable specific substrate recognition, and reduce the reaction barriers for targeted products. This results in enzyme-like reaction efficiency and selectivity. In the current phase, we are particularly interested in developing molecular cages capable of performing enzyme-like tandem catalysis, such as hydrogen evolution reactions coupled with the photooxidation of alcohols. Additionally, we are working on bioinspired cages featuring Cu centers to mimic the behavior of the particulate methane monooxygenase (pMMO) for C–H hydroxylation.
3. Photoactive Carbene Complexes for Anticancer Therapy: Photodynamic therapy (PDT) relies on photoactive drug candidates that generate reactive oxygen species (ROS) upon photoexcitation to selectively damage cancer cells. Many current PDT drugs in clinical trials are based on precious metals, which can increase the cost of treatment and pose dark toxicity risks for healthy cells. Our research focuses on the development of photoactive first-row transition metal carbene complexes that have the potential to be used in photodynamic anticancer therapy. These complexes are designed to contain only earth-abundant elements, resulting in lower dark toxicity and more affordable cancer treatment options. The abundance and synthetic versatility of carbene ligands provide ample opportunities for structural and functional modifications, enabling us to develop highly effective PDT drug candidates.

Awards

• 2018 Leon O. Morgan Fellowship, UT Austin
• 2018 Ethel Gene Kahmer Endowed Presidential Fellowship, UT Austin
• 2016 Professional Development Award, UT Austin

Selected Publications

• Z-L. Xie , N. Gupta, J. Niklas, O. G. Poleuktov, V. M. Lynch, K. D. Glusac, K. L. Mulfort. Photochemical charge accumulation in a heteroleptic copper(I)-anthraquinone molecular dyad via proton-coupled electron transfer. Chem. Sci., 2023, in press
• L. Wang, Z.-L. Xie , B. T. Phelan, V. M. Lynch, L. X. Chen, K. L. Mulfort*. Changing Directions: Influence of Ligand Electronics on the Directionality and Kinetics of Photoinduced Charge Transfer in Cu(I)Diimine Complexes. Inorg. Chem., 2023, in press
• Z.-L. Xie , X. Liu, A. J. S. Valentine, V. M. Lynch, D. M. Tiede, X. Li*, K. L. Mulfort*. Bimetallic Copper/Ruthenium/Osmium Complexes: Observation of Conformational Differences Between the Solution Phase and Solid State by Atomic Pair Distribution Function Analysis. Angew. Chem. Int. Ed., 2022, 61, e202111764. (ACIE hot paper and journal cover)
• M.W. Mara, B. T. Phelan, Z.-L. Xie , T. W. Kim, D. J. Hsu, X. Liu, A. J. S. Valentine, P. Kim, X. Li, S. Adachi, T. Katayama, K. L. Mulfort*, L. X. Chen*. Unveiling ultrafast dynamics in bridged bimetallic complexes using optical and X-ray transient absorption spectroscopies. Chem. Sci., 2022, 13, 1715-1724.
• Z-L. Xie , W. Chai, G. A. Henkelman, M. J. Rose*. Bioinspired CNP Iron(II) Pincers Relevant to [Fe]-Hydrogenase (Hmd): Effect of Dicarbonyl versus Monocarbonyl Motifs in H₂ Activation and Transfer Hydrogenation. Inorg. Chem. 2020, 59, 2548–2561.
• Z-L . Xie , D. Pennington, J. Lo, D. Boucher and M. J. Rose*. Effects of Thiolate Ligation in Monoiron Hydrogenase (Hmd): Stability of the {Fe(CO)²}²⁺ Core with NNS Ligands. Inorg. Chem. 2018. 57, 10028-10039.
• Z-L. Xie , G. Durgaprasad, A. K. Ali and M. J. Rose*. Substitution reactions of iron(II) carbamoyl-thioether complexes related to mono-iron hydrogenase. Dalton Transactions. 2017. 46, 10814-10829.
• G. Durgaprasad†, Z.-L. Xie † and M. J. Rose*. Iron Hydride Detection and Intramolecular Hydride Transfer in a Synthetic Model of Mono-Iron Hydrogenase with a CNS Chelate. Inorg. Chem. 2016, 55, 386-389. (†co-first author)