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Katherine J. FranzView profile

Professor

• Bioinorganic Chemistry
• Metal Homeostasis
• Antimicrobial Agents
• +4 more

Katherine J. Franz is a Professor of Chemistry at Duke University, affiliated with the Trinity College of Arts & Sciences and the Duke Cancer Institute. She holds a Ph.D. from MIT (2000) and a B.A. from Wellesley College (1995). Her research focuses on bioinorganic chemistry, particularly metal ion coordination in biological systems, with applications in antimicrobial therapies, cancer metallomics, and neurodegenerative diseases. Key projects include developing prochelators targeting fungal and bacterial pathogens, studying copper's role in antifungal drug efficacy, and designing light-activated metal complexes for controlled drug release. Dr. Franz has received numerous awards including the Camille Dreyfus Teacher-Scholar Award (2009), Sloan Research Fellowship (2008), and the NSF CAREER Award (2005). She leads a lab with 6 current students/mentees and has secured grants from NIH, NSF, and the US-Israel Binational Science Foundation. Her lab's work spans from fundamental metalloprotein studies to translational drug development, emphasizing interdisciplinary approaches in chemistry and biology. Education: Ph.D. in Chemistry, MIT, 2000 B.A. in Chemistry, Wellesley College, 1995 Research Interests: Metal homeostasis in pathogens, copper's role in antifungal resistance, prodrug design for targeted therapy, and mechanistic studies of metalloproteins. Grants: Tri-Institutional Molecular Mycology Training Program (NIH, 2024–2029) Duke PREP Biomedical Sciences Program (NIGMS, 2022–2027) Copper-Mucin Interaction Study (BSF, 2022–2026) Her lab's publications (n=15+ since 2020) highlight breakthroughs in prodrug selectivity, copper-induced protein toxicity, and histatin antifungal mechanisms. The Franz Lab actively collaborates with clinicians and computational scientists to advance therapeutic strategies addressing unmet medical needs in infectious diseases and cancer.

Michael KrisingerView profile

Academic

• Biochemistry
• Molecular Biology
• Coagulation
• +3 more

Michael Krisinger is an Associate Professor of Teaching in the Department of Biochemistry & Molecular Biology at the University of British Columbia . He began his teaching career in 2010, transitioning to full-time in 2013. He lectures Biochemistry 202 (Introductory Medical Biochemistry) and Biochemistry 303 (Molecular Biochemistry) while serving as a tutor in the Faculty of Medicine's Case Based Learning program. Krisinger co-developed the department's two-course summer program for international students and mentors postdoctoral fellows in teaching. He also manages the department's CANVAS digital learning platform. Krisinger's research focuses on the molecular mechanisms of coagulation and complement system regulation , particularly their evolutionary relationship and functional interplay. His work has explored thrombin's role in complement activation, polyphosphate-mediated complement suppression, and nanoparticle surface interactions with proteolytic cascades. He previously co-supervised graduate students at UBC's Centre for Blood Research before prioritizing education. Publications highlight his expertise in protease-substrate dynamics , lipoprotein-phospholipid interactions , and hemostasis-immunity crosstalk . He remains engaged in public science through community environmental initiatives and local outreach activities.

Partha BasuView profile

Professor

• Bioinorganic Chemistry
• Metalloenzymes
• Nitrogen Metabolism
• +2 more

Partha Basu is Professor and Chair of Chemistry and Chemical Biology at Indiana University Indianapolis School of Science. His bioinorganic chemistry research examines molybdenum-containing enzymes involved in nitrogen, arsenic and sulfur metabolism. He directs an interdisciplinary research group studying metal function in biological systems through biochemical and spectroscopic approaches. Research domains include: Structure-function relationships in metalloenzymes Catalytic mechanisms of molybdenum cofactor enzymes Metabolic pathways of environmental toxins Spectroscopic characterization of metal sites He has filed five patents and published over 100 peer-reviewed articles that have received approximately 5,700 citations. As founding director of the Center for Metals in Biological Systems (2005-2016), he established collaborative research infrastructure supporting metalloprotein studies.

Joseph CotruvoView profile

Professor

• Biochemistry
• Biophysics
• Catalysis
• +9 more

Joseph Cotruvo is a Professor of Chemistry at the Department of Chemistry, Pennsylvania State University. His research focuses on understanding metal selectivity in biological systems, particularly lanthanides and transition metals, with applications in biotechnology, environmental science, and disease mechanisms. He leads the Cotruvo Lab, which develops biochemical and chemical biology tools to study metal ion acquisition, trafficking, and utilization in bacteria and human pathogens. Education: Ph.D., Chemistry, Massachusetts Institute of Technology (2012); A.B., Chemistry, Princeton University (2006). Research interests include lanthanide-dependent enzymology, protein engineering for rare earth element separations, and transition metal roles in neurodegenerative diseases. The lab designs fluorescent sensors, genetically encodable tools, and protein-based systems for metal detection and recovery. Recent work emphasizes actinide/lanthanide speciation, biohydrometallurgy, and biomolecular mechanisms of metal ion transport. Notable achievements include the discovery of lanmodulin—a highly selective lanthanide-binding protein—and its application in rare earth element recovery. His lab pioneered protein-based approaches for high-purity rare earth separations and developed manganese(II) fluorescent sensors. Research also explores iron-responsive riboswitches and copper-regulated lipid metabolism. Awards: Faculty Scholar Medal (2025), Blavatnik Finalist (2024), Eli Lilly Award (2024), Sloan Fellowship (2021), DOE Early Career Award (2020). Grants: NSF CAREER Award, Charles E. Kaufman Foundation, Jane Coffin Childs Memorial Fund. Labs/Teams: Cotruvo Lab (Penn State); collaborations with National Synchrotron Light Source, Lawrence Livermore National Laboratory. Future work targets scalable rare earth recovery systems, actinide-biomolecule interactions, and transition metal roles in infectious diseases.

• Biochemistry
• Structural Biology
• Molecular Biophysics
• +4 more

Alessandra Pesce is an Associate Professor at the Department of Physics (DIFI) of the University of Genoa, Italy. Her research focuses on structural biology of globins, protein aggregation, and cold-adapted enzymes, with applications in life sciences, environmental monitoring, and cultural heritage preservation. She teaches Applied Physics and Biophysics at both undergraduate and graduate levels in Physics and Biological Sciences. Her work spans from atomic-level characterization of protein crystals using Atomic Force Microscopy to large-scale ecological projects like the LIFE+ WHALESAFE initiative for sperm whale conservation through acoustic monitoring. Email: alessandra.pesce@unige.it Phone: +39 010 33 56243 Research Interests: Structural characterization of hexa-coordinated globins in marine organisms Thermodynamic and kinetic analysis of truncated hemoglobins in pathogenic bacteria Quaternary structure adaptations in Antarctic enzymes Development of acoustic monitoring systems for marine mammal conservation Protein aggregation mechanisms in amyloid-related diseases Publication Trends: Over 15 years, her research demonstrates expertise in combining X-ray crystallography with biophysical techniques to study globin family proteins across diverse species (from nematodes to whales). Key themes include heme reactivity modulation, ligand diffusion pathways, and structure-function relationships in extremophile proteins, with recent emphasis on marine conservation technology.

Peter Z. QinView profile

Professor

• Physical Chemistry
• Biochemistry
• CRISPR Technology
• +3 more

Professor Peter Z. Qin is a faculty member in the Department of Chemistry at the University of Southern California (USC), affiliated with the USC Dornsife College of Letters, Arts and Sciences. His research focuses on understanding nucleic acid recognition mechanisms, genome engineering, and CRISPR-Cas systems, employing advanced techniques like Site-Directed Spin Labeling (SDSL) and electron paramagnetic resonance (EPR) spectroscopy. Qin earned his Ph.D. from Columbia University (1999) and B.S. from Peking University (1991). Research interests include structural dynamics of nucleic acids, protein-nucleic acid interactions, and CRISPR-mediated DNA cleavage mechanisms. His work bridges physical chemistry and biochemistry, with applications in diagnostics, therapeutics, and gene editing. Notable contributions involve elucidating CRISPR-Cas9 and Cas12a mechanisms, DNA-unwinding checkpoints, and the role of bridge helices in target discrimination. Recent publications (2021–2025) emphasize CRISPR-Cas systems, DNA dynamics, EPR-based instrumentation, and molecular mechanisms of genome editing. His group develops tools like dual-mode EPR spectrometers and phosphorothioate-based RNA labeling techniques. The lab actively publishes in high-impact journals and collaborates on translational projects like CRISPR-engineered mouse models. Prof. Qin’s work is supported by grants and collaborations, though specific funding details are not listed. His lab maintains a dedicated website detailing ongoing research and methodologies.

Donovan C. HainesView profile

Professor

• Bioorganic Chemistry
• Biophysics
• Enzymology
• +5 more

Donovan C. Haines serves as Professor and Chair of the Department of Chemistry at Sam Houston State University within the College of Science & Engineering Technology. His extensive academic career includes previous positions as Assistant Professor and Associate Professor at both the University of Texas at Dallas and Sam Houston State University, culminating in his current professorship and chairmanship since 2020. Haines' research spans multiple interconnected fields focusing on the structure and mechanism of monooxygenase systems, particularly cytochrome P450 enzymes involved in metabolism of natural products, neurotransmitters, drugs, and hormones. His work has direct medical relevance to neurodegenerative diseases including ALS, Parkinson's, and Alzheimer's. Specific research areas include bacterial quorum sensing, forensic chemistry related to human decomposition, and lipid metabolism enzymes connected to immune function and skin disorders. Analysis of his 15 most recent publications reveals a strong focus on cytochrome P450 enzymology, with significant work on bacterial quorum sensing mechanisms, forensic applications, and protein structure-function relationships. His research demonstrates consistent interdisciplinary collaboration across biochemistry, microbiology, and forensic science. Haines maintains an active research program with publications spanning over two decades, with his most recent work expanding into aerospace medicine with research on remains containment in low-earth orbit. His scientific contributions demonstrate both depth in specialized enzymology and breadth across multiple application domains. As an educator, Haines teaches across the chemistry curriculum from introductory courses to advanced biochemistry, demonstrating commitment to both undergraduate and graduate education. His laboratory employs diverse methodologies including organic synthesis, biochemistry, molecular biology, and biophysics to study enzyme mechanisms.

Sean J. ElliottView profile

Professor

• Bioinorganic Chemistry
• Catalysis Sciences
• Metalloprotein Structure:Function Relationships
• +3 more

Sean J. Elliott is a Professor at Boston University's Chemistry Department, with an affiliated role in the Division of Materials Science and Engineering. He leads the Elliott Group, focusing on catalysis sciences and metalloprotein structure:function relationships. His research integrates electrochemistry and spectroscopy to study environmental transformations of nitrogen, carbon, oxygen, and sulfur. Education: Ph.D. in Bioinorganic Chemistry from Caltech (2000). Honors include the Scialog Award (2010/2011), Gitner Award for Distinguished Teaching (2007), and NSF CAREER Award (2005). Research emphasizes electrocatalytic systems, such as nitrite reduction to ammonia using cytochrome c nitrite reductase and light-driven CO₂ reduction via ferredoxin networks. His lab explores enzyme mechanisms, redox carriers, and biogeochemical cycles. Publications highlight advancements in enzyme-catalyzed reactions, metalloprotein structure-function relationships, and bioelectrochemical systems. He collaborates on interdisciplinary projects involving microbial metabolism and environmental chemistry. Labs/Teams: The Elliott Group (http://sites.bu.edu/sje-lab) investigates bioenergetics, enzymology, and electrochemical interfaces in biological systems. His work bridges fundamental biochemistry with applied catalysis for sustainable energy solutions.

• Biocatalysis
• Protein Engineering
• Non-Canonical Amino Acids
• +5 more

Ivana Drienovska is an Assistant Professor in the Department of Chemistry and Pharmaceutical Sciences at the Faculty of Science, Vrije Universiteit Amsterdam . She also holds an affiliation with AIMMS (likely a research institute or program). Her research focuses on biocatalysis, protein engineering, and artificial enzyme design , with a particular emphasis on non-canonical amino acids, genetic code expansion, and functional group diversity in enzymes. She explores applications in sustainable chemistry, enzyme stabilization, and novel catalytic mechanisms. Recent work includes designing protein scaffolds for iminium biocatalysis, stabilizing protein complexes via covalent bicyclization, and incorporating functional secondary amines via genetic code expansion. Her studies often involve structural biology approaches (e.g., crystallography) and synthetic biology techniques. Affiliations : Faculty of Science (VU Amsterdam), AIMMS Courses Taught : Biocatalysis for a Sustainable Future, Bioorganic Chemistry, Concepts in Chemical Biology Key Research Themes : Engineering enzymes for novel functionalities (e.g., unnatural amino acids) Development of artificial metalloenzymes for asymmetric catalysis Structural and biochemical analysis of cold-adapted and extremophilic enzymes Lab/Team : Her group works at the interface of chemical biology, enzymology, and synthetic biology, focusing on creating next-generation biocatalysts for industrial and environmental applications.

Claudia AndreiniView profile

Associate Professor

• Metalloproteins
• Bioinformatics
• Biological Databases
• +3 more

Claudia Andreini is an Associate Professor at the University of Florence, affiliated with the Magnetic Resonance Center and the Department of Chemistry. Her research focuses on computational biology, particularly metalloproteins and bioinformatics. She pioneered the use of bioinformatics to study metalloproteins and developed the MetalPDB database. She collaborates internationally and has presented at major conferences. Education: PhD in Chemistry (2006), University of Florence; Laurea in Chemistry (2002, cum laude), University of Florence. Research interests include metalloprotein structure-function relationships, metal-coordination databases, and predictive computational tools. Her work integrates structural bioinformatics, machine learning, and database mining to analyze metal sites in proteins. Recent publications highlight advancements in zinc-binding site prediction, metal-induced structural variability, and applications of deep learning in metalloprotein analysis. She has contributed to drug design studies involving ruthenium complexes and antibacterial agents. No scientific awards or grants are explicitly listed in the provided texts. She leads the MetalPDB project and collaborates on structural biology initiatives.

Miguel A. De la RosaView profile

Professor

• Structural biology
• Biophysics
• Bioinorganic chemistry
• +2 more

Miguel A. De la Rosa is a Full Professor of Biochemistry and Molecular Biology at the University of Seville since 1995. His academic career spans leadership roles including Director of cicCartuja Scientific Research Center (2009-18) and Secretary General of FEBS (2023-). He also served as Visiting Professor at the University of Arizona (1990-94). Education : M.Sc. (1st class honours, 1977) and Ph.D. (cum laude, 1981) in Biochemistry from the University of Seville. Research interests focus on structure-activity relationships of biological macromolecules, particularly protein-protein and protein-nucleic acid interactions. His work employs interdisciplinary approaches from molecular biology to computational chemistry, with major achievements in metalloprotein evolution, electron transfer mechanisms in photosynthesis/respiration, and cytochrome c's role in DNA damage and programmed cell death. Publication trends emphasize cytochrome c modifications (phosphorylation, acetylation), electron transfer dynamics, structural analysis of redox proteins, and mitochondrial dysfunction. His studies bridge structural biology, biophysics, and molecular mechanisms of cell death. 2025 FAMA Prize for scientific career 2019 Honorary Member of SEBBM 2019 Elected Member of Academia Europaea FEBS National Lecture Award (2010) He has supervised more than 20 PhD students and 20 postdocs, co-founded spin-off ManSciTech S.L. , and directed large-scale interdisciplinary projects at CSIC-University of Seville institutes.

• Crystallography
• Biocrystallography
• Structural Chemistry
• +4 more

Geremia Silvano is an Associate Professor of General and Inorganic Chemistry at the Department of Chemistry and Pharmaceutical Sciences, University of Trieste. He serves as Head of the Department and coordinates the Center of Excellence in Biocrystallography (CEB). As a member of multiple doctoral boards (Cycles XXIX through XXXIX), he plays a significant role in graduate education at the university. His educational background includes a Degree in Chemistry from Trieste (1988) and a PhD in Chemical Sciences (1992). His academic career progressed from Assistant Professor positions in Ancona (1994) and Trieste (1996) to Associate Professor (2002), with research experience at Oxford's Laboratory of Molecular Biophysics. Professor Silvano's research focuses on structural studies of supramolecular and protein systems using crystallographic techniques. His work spans several key areas: Biocrystallography of natural and artificial proteins Structural analysis of redox proteins Host-guest chemistry in supramolecular systems Vitamin B-12 chemotherapeutic agents and bioconjugates His publication record includes approximately 180 works in high-impact journals (H-index = 37), with research utilizing synchrotron radiation facilities worldwide including SRS (UK), LURE (France), ESRF (France), HASYLAB (Germany), and Elettra (Italy). Professor Silvano has supervised 6 PhD theses and numerous Bachelor's and Master's theses. He serves as a referee for international journals and as a valuator of research projects. His administrative roles include membership in the Commission for drafting the UniTS Statute (2011), the Administrative Council of the University College for Sciences 'L. Fonda' (2012), and the Academic Senate of UniTS (2012).

Catherine DrennanView profile

Professor

• Metalloenzyme Biochemistry
• Structural Biology
• Enzyme Catalysis
• +4 more

Catherine Drennan is a Professor of Biology and Chemistry at MIT and an Investigator/Professor at the Howard Hughes Medical Institute (HHMI). She leads the Drennan Research Laboratory, focusing on structural and biochemical studies of metalloenzymes involved in medically and environmentally significant processes. Her work combines X-ray crystallography and cryo-electron microscopy to investigate enzyme mechanisms and conformational changes in catalysis. Education PhD in Chemistry, University of Michigan (1995) BS in Chemistry, Vassar College (1985) Research Interests Her lab explores metalloprotein biochemistry, particularly in enzymes critical for environmental remediation and human health. Key areas include: Structure-function relationships in ribonucleotide reductases Mechanisms of glycyl radical enzymes Role of metal cofactors (iron, nickel) in catalysis Impact of conformational dynamics on enzyme activity Recent Trends in Publications Recent work highlights advances in cryo-EM structural analysis of ribonucleotide reductases and carbon monoxide dehydrogenases, revealing insights into enzyme regulation and inhibitor mechanisms. Studies also address the role of metallochaperones in cofactor insertion and the structural basis of enzymatic reactions like indole nitrile formation. Awards Member, National Academy of Sciences (2023) Fellow, American Society for Biochemistry and Molecular Biology (2021) Howard Hughes Medical Institute Investigator (2008) Grants & Advising Her research is supported by HHMI and NIH grants. She mentors students/postdocs in structural biology and enzyme mechanisms, emphasizing both experimental and computational approaches. Labs & Collaborations The Drennan Lab collaborates with institutions globally, focusing on advancing structural biology techniques and applying them to unresolved enzymatic mechanisms. The lab also develops educational resources for undergraduate science teaching.

• Biochemistry
• Protein Science
• Enzymology
• +3 more

Hegne Pupart is an Engineer at Tallinn University of Technology's School of Science, Department of Chemistry and Biotechnology since September 1, 2024. Previously, she served as a Junior Research Fellow (40% position) at the same institution from September 2019 to August 2024. She recently completed her Doctoral Degree in 2024 with her dissertation titled "Characterization of Bacterial Dye-Decolorizing Peroxidases," supervised by Tiit Lukk, Priit Eek, and Priit Väljamäe. She also holds a Master's Degree from 2019 with her thesis on "Expression and Purification of Human Superoxide Dismutase 1." Dr. Pupart's research focuses on protein biochemistry, particularly: Biochemistry and enzymology of peroxidases Lignin degradation and remodeling Protein structure-function relationships Metalloprotein characterization Her recent publications demonstrate expertise in bacterial dye-decolorizing peroxidases, particularly from Streptomyces coelicolor and Thermobifida species. Her work examines enzyme kinetics, oligomerization states, and applications in lignin degradation. She has also contributed to research on superoxide dismutase and Alzheimer's-related protein aggregation, showing a diverse research portfolio spanning fundamental enzymology to biomedical applications. Dr. Pupart is currently involved in the "Structural determinants of protein techno-functional properties" project (2024-2028), funded by the Estonian Research Council with 1,088,843 EUR, where she works under Principal Investigator Priit Eek. This project represents a continuation of her doctoral work on protein structure-function relationships.

Raphael LedermannView profile

Researcher

• Microbiology
• Plant-Microbe Interactions
• Symbiosis
• +3 more

Dr. Raphael Ledermann is a Post-Doc Researcher at the University of Oxford, affiliated with the Rhizosphere Group. His research focuses on the molecular mechanisms underlying Rhizobium-legume symbioses, particularly how bacteria and plants coordinate metabolism and physiology to establish mutualistic nitrogen-fixation interactions. His work addresses symbiosis adaptation, environmental stress responses, and microbial community dynamics in plant-associated niches. Contact details include his email raphael.ledermann@biology.ox.ac.uk and professional profiles on ResearchGate (Orchid ID: B-4301-2018). His research portfolio spans microbiology, plant biology, and systems approaches to understand symbiotic relationships and bacterial adaptation strategies. Key research themes include nitrogen fixation mechanisms, bacterial stress responses (osmotic/salt), microbial community assembly, and symbiotic signaling pathways. His recent findings highlight roles of metabolic enzymes, hopanoids, and chemical chaperones in enabling symbiotic success under environmental challenges. Publications (2014-2025) reflect interdisciplinary approaches combining molecular genetics, biochemistry, and systems biology to elucidate symbiosis at cellular and ecological scales. While no awards are explicitly listed, his work contributes foundational insights to legume-microbe symbiosis research.