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Prof. Susanne Kassube is an SNSF Assistant Professor in the Department of Biochemistry at the University of Zurich, affiliated with the Faculty of Science. Her research focuses on the molecular mechanisms of Fe-S protein biogenesis and DNA repair enzymes, employing structural biology techniques such as cryo-electron microscopy and X-ray crystallography alongside biochemical and biophysical methods. She holds a Ph.D. in Biophysics from the University of California, Berkeley (2013), and completed postdoctoral training at the Friedrich Miescher Institute for Biomedical Research in Basel (2014–2020). Education: Diploma (M.Sc.) in Biology, University of Heidelberg, Germany (2008) Ph.D. in Biophysics, University of California, Berkeley, USA (2013) Research Interests: Fe-S cluster assembly and dysfunction in human diseases Mechanisms of DNA repair proteins Structural biology of large macromolecular machines Her work integrates structural and functional studies to elucidate how Fe-S clusters regulate cellular processes like DNA repair and oxidative stress response. Awards: SNSF PRIMA Grant (2021) EMBO Long-Term Postdoctoral Fellowship (2015) Boehringer Ingelheim Fonds PhD Fellowship (2010) Advising & Grants: Advises PhD students (Roberta Cadei, Keshav Goyal, Steffen Winkler) and a Master’s student (Anna von Wyss). Recipient of the SNSF PRIMA Grant supporting her research into Fe-S protein biogenesis. Labs/Teams: The Kassube Group at the University of Zurich focuses on structural and biochemical studies of Fe-S proteins and DNA repair mechanisms. Team members include lab technicians and technical staff.

• Biochemistry
• Structural Biology
• Molecular Biology
• +3 more

F. Wayne Outten is a Professor in the Department of Chemistry and Biochemistry at the University of South Carolina, affiliated with the McCausland College of Arts and Sciences. He holds the Guy F. Lipscomb, Sr. Professorship of Biochemistry. His research focuses on microbial metal metabolism, particularly Fe-S cluster biogenesis under stress conditions and metal homeostasis in bacteria. He has authored over 40 peer-reviewed publications and secured significant NIH and NSF funding. Education: B.S. in Biology (College of William and Mary, 1995); Ph.D. in Biochemistry (Northwestern University, 2001); Postdoctoral Fellowship at NIH (2001–2005). Awards include the Cottrell Scholar Award and Ada B. Thomas Advisor Award. Research Interests: Iron and copper homeostasis, oxidative stress responses, bacterial pathogenesis, and Fe-S cluster assembly pathways (Suf system). Key contributions include defining roles of SufBCD and SufE proteins in Fe-S cluster formation under iron starvation and oxidative stress. Grants: Current NIH support for studying Fe-S cluster dynamics and NSF funding for membrane biogenesis integration with metal metabolism. Collaborative projects include designing pH-responsive ferritin nanocages for drug delivery. Labs: GSRC 303, 304, 320, 321. Active in professional societies (ASBMB, ACS) and conference organization (Iron-Sulfur Biogenesis). Mentored 23 undergraduates, 16 Ph.D. students, and 3 postdocs. Military service includes roles in U.S. Army Reserve and National Guard.

• Microbial Metal Metabolism
• Bioinorganic Chemistry
• Microbial Physiology
• +7 more

Patrick A. Frantom is a Professor in the Department of Chemistry and Biochemistry at The University of Alabama. His research integrates biochemical, bioinformatic, and biophysical techniques to study enzyme structure, function, and evolution. He leads projects funded by the NIH (R01-GM112919) and NSF CAREER Award, focusing on Fe-S cluster biogenesis and glycosyltransferase mechanisms. Education : PhD from Texas A&M University (2005), Postdoctoral Fellow at Albert Einstein College of Medicine (2005-2009) Research highlights include: Investigating conformational dynamics and allosteric regulation in the Suf Fe-S cluster biogenesis pathway, critical for bacterial survival under oxidative stress. Exploring functional diversity in glycosyltransferase enzymes through structural and mechanistic studies using HDX-MS and bioinformatics. Collaborative work with experts like Dr. Jack Dunkle (UA) and Dr. Wayne Outten (University of South Carolina). His lab employs advanced instrumentation including a Waters Xevo QToF mass spectrometer with HDX Manager UPLC system. Scientific Awards : NSF CAREER Award MCB-1254077 The Frantom Lab actively engages in graduate training and is part of the broader University of Alabama research ecosystem.

• Mechanistic Enzymology
• Protein Structure-Function Relationships
• Fe-S Cluster Biogenesis
• +3 more

Dr. Tracey A. Rouault is a Physician Scientist leading the Section on Human Iron Metabolism at the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD), part of the National Institutes of Health (NIH) in Bethesda, MD. Her research focuses on the molecular regulation of iron and iron-sulfur cluster metabolism in mammalian systems. Research Interests: Dr. Rouault’s lab investigates the roles of iron regulatory proteins (IRPs) and iron-sulfur cluster biogenesis in health and disease. Her work spans neurodegenerative disorders such as Parkinson’s disease and Friedreich ataxia, hematologic conditions including anemias and polycythemia, and familial renal cancers. The lab employs mouse models, cell culture, and patient-derived lines to dissect the mechanisms of iron homeostasis and mitochondrial function. Recent Research Trends: Analysis of her recent publications reveals a strong focus on the role of iron-sulfur clusters in metabolic reprogramming, immune cell function, and epigenetic regulation. Her work continues to uncover novel protein complexes and regulatory motifs involved in Fe-S cluster assembly and iron transport, with implications for understanding and treating rare genetic and metabolic diseases. Scientific Awards: No specific awards mentioned in the provided text. Advising and Grants: Dr. Rouault mentors post-doctoral and graduate fellows. Opportunities are available through the NIH Graduate Partnership Program with universities such as Johns Hopkins, University of Maryland, Oxford, and Cambridge. Her research is supported by the NIH intramural funding program, indicating ongoing grant support for her lab’s investigations into iron metabolism and related disorders. Labs and Teams: She leads the Section on Human Iron Metabolism within NICHD, conducting interdisciplinary research that bridges biochemistry, genetics, and physiology to understand fundamental aspects of iron biology and their clinical implications.

• Iron Metabolism
• Iron-Sulfur Cluster Biogenesis
• Neurodegenerative Diseases
• +7 more

Deborah Perlstein is an Associate Professor at Boston University, with research spanning the intersection of chemistry and biology. Her work focuses on bioinorganic chemistry , particularly the biophysical and biochemical mechanisms of iron-sulfur cluster-containing proteins and bacterial cell division . She employs techniques such as enzymology , microscopy , and molecular biology to dissect these systems. Education: B.S. in Biological Chemistry, Tulane University (1998) Ph.D. in Biochemistry, Massachusetts Institute of Technology (2005) Postdoctoral Fellowship in Microbiology and Chemical Biology, Harvard Medical School (2010) Research Interests delve into: Iron-Sulfur Proteins: Ancient cofactors enabling non-standard amino acid chemistries. Key goals include elucidating enzymatic mechanisms and in vivo assembly pathways for these clusters. Bacterial Cell Division: Targeting cytoskeletal proteins like MreB and FtsZ to develop antibiotics against drug-resistant pathogens. Studies include protein dynamics regulation in vitro and in vivo. Publications highlight her contributions to understanding iron-sulfur cluster maturation, ATPase roles, and bacterial growth mechanisms. Recent work integrates machine learning for experimental biochemists and structural studies of scaffold proteins like Met18. Students include undergraduates and summer researchers such as Darlene S. Douglas (MIT, B.S. 2001) and Mia Lassier (Harvard Summer Program, 2009). Contact: Email dperl@bu.edu | Phone 617.358.6180

• Bioinorganic Chemistry
• Chemical Biology
• Iron-Sulfur Cluster Biology
• +4 more

Professor Kostas Tokatlidis is the Cathcart Chair of Biochemistry and Director of Research in the School of Molecular Biosciences at the University of Glasgow, where he heads the Mitochondria Biology Laboratory. He is an elected Member of EMBO, Academia Europaea, Fellow of the Royal Society of Edinburgh (FRSE), Royal Society of Chemistry (FRSC) and Royal Society of Biology (FRSB). Education & Training PhD in Biochemical Engineering, University of Delaware, USA (1988–1993) – Fulbright Fellow Post-doctoral fellowships: Institut Pasteur, France (1993–1994); Biozentrum, Switzerland (1994–1998) First-class BSc in Chemical Engineering, Aristotle University of Thessaloniki, Greece Major research interests Mitochondrial biogenesis and protein import pathways Oxidative protein folding and redox signalling Molecular chaperones and membrane protein assembly Stress responses, metabolism and ageing Iron–sulfur cluster biogenesis and disease links Scientific awards & honours 2022 – Member, Academia Europaea 2021 – Fellow, Royal Society of Chemistry (FRSC) 2020 – Fellow, Royal Society of Biology (FRSB) 2016 – Fellow, Royal Society of Edinburgh (FRSE) 2013 – EMBO Member & Royal Society Wolfson Research Merit Award 2012 – Greek Ministry of Education Excellence Grant 2001 – Lister Institute Research Fellow & MRC Career Establishment Award 1988 – Fulbright Fellow Advising & Grant leadership He has mentored 25 PhD/graduate students and 17 post-doctoral researchers and has served as Director of Graduate/Undergraduate Studies and Director of Research in the School of Molecular Biosciences. His group has secured >€12 million in competitive funding from 43 UK/EU grants, including current awards such as the 2025-2031 EPSRC MAINSTREAM Hub, MRC Mitotrapin and BBSRC partnership grants. Laboratory & facilities Professor Tokatlidis leads the Mitochondria Biology Laboratory and the Mitochondrial Analysis Facility at the University of Glasgow, coordinates the Scottish Healthy Ageing and Mitochondria & Redox Biology research networks, and fosters interdisciplinary collaborations across Europe and globally.

• Mitochondria biogenesis
• Protein targeting and import
• Protein folding and assembly
• +4 more

Patricia C. Dos Santos is a Professor in the Department of Chemistry at Wake Forest University, located in the College of Arts and Sciences. She conducts active research on the biochemical mechanisms of iron-sulfur cluster assembly in Gram-positive bacteria, a fundamental process in cellular metabolism and metalloprotein function. Her educational background includes a B.S. from Universidade Federal do Rio Grande do Sul (1999, Brazil) and a Ph.D. from Virginia Tech (2004), followed by postdoctoral training at the same institution under Dennis Dean. Dr. Dos Santos's research lies at the intersection of biochemistry, microbiology, and inorganic chemistry, with a focus on metalloenzymes and metal cofactor biosynthesis. Her work contributes to understanding essential life processes such as respiration, carbon metabolism, and nitrogen fixation through the lens of [Fe-S] cluster biogenesis. Although specific publications are not listed in the provided text, her research output is recognized through sustained funding and scholarly recognition, indicating a strong publication record in bioinorganic and microbial biochemistry. URECA Faculty Award for Excellence in Mentorship in Research (2020) Robert & Debra Lee Faculty Fellowship (2018-2021) Freiburg Institute for Advanced Sciences Fellow (2018-2019) Z. Smith Reynolds Foundation Faculty Fellowship (2013-2016) Faculty Excellence in Research Award, Wake Forest University (2013) NSF CAREER Award (2011) Outstanding Recent Alumna, Virginia Tech (2010) Dr. Dos Santos is actively involved in mentoring undergraduate and graduate researchers, as evidenced by the URECA mentorship award. She has secured competitive grants including the NSF CAREER Award and multiple university-level fellowships, supporting her research program and student training. While specific grant titles are not listed, the funding sources reflect strong institutional and national recognition of her research potential and productivity. She leads a research group investigating the biochemical pathways of [Fe-S] cluster formation in bacteria, likely involving interdisciplinary collaboration and laboratory-based experimentation in chemical and molecular biology.

• Bioinorganic Chemistry
• Metalloprotein Biochemistry
• Iron-Sulfur Cluster Biogenesis
• +5 more

Justin Wilson is a Professor of Chemistry & Biochemistry at the University of California, Santa Barbara (UCSB), affiliated with the College of Letters and Science. He holds a PhD from MIT (2013) and a BS from UC Berkeley (2008). His research focuses on bioinorganic chemistry, radiochemistry, and f-element coordination chemistry, with applications in anticancer drug design, radiopharmaceuticals, and mitochondrial calcium uniporter inhibition. Key projects include developing chelating agents for radiometals, designing inhibitors for ischemia-reperfusion injury, and exploring rare earth element separations. Wilson’s awards include the Cottrell Scholar Award (2017), Jonathan Sessler Award (2019), and the National ACS Harry Gray Award (2022). His lab has produced over 100 publications, emphasizing interdisciplinary approaches to medicinal and nuclear chemistry. Notable students include Zhouyang Huang, Nicholas Bigham, and Yangyang Gao. The lab collaborates with institutions like Los Alamos National Laboratory and Cornell University, advancing translational research in diagnostics and therapeutics. Education: PhD in Inorganic Chemistry (MIT, 2013); BS in Chemistry (UC Berkeley, 2008). Professional milestones include tenure at Cornell (2021) and a faculty position at UCSB (2024). Research highlights include Ru265, a mitochondrial calcium uniporter inhibitor, and Py-Macrodipa, a dual-size chelator for radiometals. The lab also engages in undergraduate education through nuclear chemistry experiments and outreach programs like 'Radioactive World.'

• Bioinorganic Chemistry
• Radiochemistry
• F-element Coordination Chemistry
• +5 more

Prof. Dr. Michael Bott is a Professor of Biotechnology at the University of Düsseldorf and Director of the Institute of Bio- and Geosciences (IBG-1: Biotechnology) at Forschungszentrum Jülich. His research focuses on molecular microbiology and applied biotechnology, emphasizing metabolic engineering, microbial cell factories, and sustainable bioeconomy applications. His work combines systems biology approaches with metabolic pathway optimization to develop industrial processes using renewable resources. Education: PhD in Biology from University of Marburg (1987), habilitation at ETH Zurich (1998). He has held leadership roles since 2007, leading cross-disciplinary projects like BacHBerry (biosynthesis of plant-derived phenolics) and AutoBioTech (automated strain engineering platforms). His research integrates high-throughput screening, adaptive laboratory evolution, and robotic systems to accelerate strain development. Key Projects: Co-culture engineering (CoNoS), microbial inositol production, 5-ketofructose synthesis, and enzyme engineering. Technological Contributions: Development of biosensors for NADPH monitoring and novel subtilisin enzymes. Publications: Over 150 peer-reviewed articles focusing on C. glutamicum systems biology and industrial applications. Laboratory activities include the Systems Microbiology group (IBG-1) and collaborations with Helmholtz institutes. His work bridges fundamental microbiology with industrial biotechnology to address challenges in renewable resource utilization and drug production.

• Molecular Microbiology
• Applied Microbiology
• Metabolic Engineering
• +3 more

Professor Judy Hirst is a leading figure at the University of Cambridge , serving as Director of the Medical Research Council Mitochondrial Biology Unit (MRC-MBU) and holding the Professor of Biological Chemistry title. Her research integrates structural, biochemical, and chemical approaches to decode energy conversion mechanisms in complex redox enzymes, particularly mitochondrial respiratory complex I , with implications for human diseases. She is a Fellow of the Royal Society (2018) and the Academy of Medical Sciences (2019) . Education: MA and DPhil in Chemistry from the University of Oxford Postdoctoral: Wellcome Trust Prize International Fellowship at The Scripps Research Institute Her work focuses on complex I's catalytic mechanisms , reactive oxygen species (ROS) production , and mitochondrial dysfunction in diseases. She pioneers electron cryomicroscopy (cryo-EM) to determine structures of energy-transducing enzymes. Her articles highlight trends in mitochondrial biogenesis , drug inhibition , and redox-driven pathologies . Scientific Awards : Fellow of the Royal Society (FRS, 2018) Fellow of the Academy of Medical Sciences (FMedSci, 2019) Wellcome Trust Prize International Fellowship She advises on Natural Sciences (Chemistry) as Director of Studies and acts as a Sustainability Adviser at her college. Her lab's integration with clinical institutions like the NHS underscores the translational impact of her research on mitochondrial diseases and therapeutic development .

• Mitochondrial Biology
• Structural Biochemistry
• Energy Conversion
• +5 more

Brendan T. Wanta, MD is a Mayo Clinic physician scientist affiliated with the Department of Anesthesiology and Perioperative Medicine . His clinical focus spans critical care , liver transplantation , and infection control in surgical environments. Dr. Wanta completed his MD (2011) at Medical College of Wisconsin Critical Care Fellowship (2016) at Mayo School of Graduate Medical Education Anesthesiology Residency (2015) at Mayo Clinic with honors including the 2025 Distinguished Clinician Award and 2021 Catalyst Award . Research interests include UV-C disinfection technologies Operating room infection control Iron-sulfur cluster biogenesis with publications in journals like Cureus and J Cardiothorac Vasc Anesth . He actively contributes to resident education and curriculum development at Mayo Clinic. Scientific accolades include Alpha Omega Alpha Honor Society membership (2010) Foundation Fellowship in Government Service (2008) Michael J. Dunn Achievement Award (2011) alongside multiple clinician and educator of the year recognitions.

• Critical Care
• Anesthesiology
• Infection Control
• +4 more

Paul Sigala is an Associate Professor of Biochemistry at the University of Utah, where he investigates the unique biochemical and cellular mechanisms of Plasmodium falciparum parasites during human erythrocyte infection. His work bridges cell biology, genetics, and chemical biology to uncover novel therapeutic strategies against malaria. Ph.D. from Stanford University Postdoctoral training at Washington University in St. Louis Research Focus: The Sigala lab specializes in dissecting parasite organelle metabolism, particularly the apicoplast and mitochondrion, and elucidating heme acquisition pathways. Their interdisciplinary approach combines CRISPR/Cas9 genome editing, in vitro biochemistry, and comparative studies in yeast/bacteria. Publication Trends: Recent studies highlight work on cytochrome maturation (2023-2025), isoprenoid dependencies (2022-2023), and divergent metabolic adaptations in malaria parasites (2017-2025). Collaborative projects span chemical probes, organelle-specific stress responses, and non-canonical protein functions. Lab Mission: The Sigala lab emphasizes inclusivity, mentorship, and collaborative problem-solving while advancing fundamental understanding of parasite biology at the intersection of host-pathogen interactions and eukaryotic evolution.

• Malaria Parasitology
• Biochemistry
• Cell Biology
• +3 more

Rafał Dutkiewicz is Professor in the Department of Evolutionary Biochemistry at the University of Gdańsk's Intercollegiate Faculty of Biotechnology. His research examines iron-sulfur cluster biogenesis mechanisms in proteins, focusing on the roles of chaperone systems in cluster assembly and transfer. His work has revealed fundamental processes in mitochondrial Fe-S protein maturation and characterized interactions between key proteins in cluster biosynthesis pathways. Recent publications explore ISC machinery mechanisms and chaperone functions in metalloprotein biogenesis.

• Iron-Sulfur Cluster Biogenesis
• Protein Folding
• Molecular Chaperones
• +1 more

Frédéric Barras is a **Researcher** and **Head of the Stress Adaptation and Metabolism (SAMe) group** at the **Department of Microbiology, Institut Pasteur (Paris, France)**. His research focuses on bacterial stress adaptation, particularly iron-sulfur (Fe-S) cluster biogenesis and their role in cellular homeostasis. Barras leads projects investigating Fe-S cluster systems' evolution, antibiotic resistance mechanisms, and microbial metabolic responses to environmental stressors. Research Interests : His work integrates molecular microbiology, biochemistry, and evolutionary genomics to study Fe-S cluster pathways in bacteria, including the ISC, SUF, SMS, and MIS systems. Key areas include redox biology, metabolic versatility, and the interplay between bioenergetics and pathogenesis. Grants & Projects : He coordinates ANR-funded projects like ANR-FirstFeS exploring ancestral Fe-S biogenesis systems and collaborates in intra-institutal initiatives like the Institut Pasteur-Weizmann Joint Research Program . His lab also investigates mechanisms underlying antibiotic resistance and microbial adaptation. Labs/Teams : Head of the SAMe group, part of the Department of Microbiology, and affiliated with the Institut Pasteur's multidisciplinary research network.

• Bacterial Stress Adaptation
• Iron-Sulfur Clusters
• Microbial Metabolism
• +3 more

Simone Ciofi Baffoni is an Associate Professor at the University of Florence, affiliated with the Magnetic Resonance Center and Department of Chemistry. His research focuses on structural biology, particularly copper trafficking, iron-sulfur protein biogenesis, and mitochondrial protein import. He employs advanced NMR spectroscopy techniques to study metalloprotein interactions and cellular mechanisms underlying human diseases. Key projects include elucidating copper distribution pathways, oxidative protein folding in mitochondria, and Fe/S cluster assembly defects. His work integrates structural biology with biochemical and biophysical methods, contributing to understanding diseases linked to metal homeostasis and mitochondrial dysfunction. He co-authored over 79 peer-reviewed publications, including high-impact journals like Nature and Nature Chemical Biology. Ciofi Baffoni is actively involved in Instruct-ERIC, a European structural biology infrastructure. Research highlights include discoveries on MIA40-mediated oxidative folding, CuA assembly mechanisms, and the role of anamorsin in Fe/S cluster biosynthesis. His lab investigates mitochondrial disorders caused by protein misfolding and cluster assembly failures, with implications for neurodegenerative and metabolic diseases. Publications emphasize structural insights into proteins like Cox17, Sco2, and NFU1, using techniques like in-cell NMR and paramagnetic spectroscopy. He has pioneered studies on [2Fe-2S] and [4Fe-4S] clusters, their transfer pathways, and disease mutations affecting these systems.

• Structural Biology
• NMR Spectroscopy
• Copper Trafficking and Homeostasis
• +3 more