
J. Martin Bollinger
· Professor of Chemistry; Professor of Biochemistry and Molecular BiologyPennsylvania State University · Biochemistry and Molecular Biology
Active 1963–2025
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About
J. Martin Bollinger is a Professor of Chemistry and Biochemistry and Molecular Biology at The Pennsylvania State University. His research focuses on the mechanisms of metalloenzymes and metallofactor assembly. He is affiliated with the Molecular, Cellular, and Integrative Biosciences program and is involved in various institutes and centers related to bioremediation, infectious disease, industrial biotechnology, and neuroscience. His work includes studying heme oxygenase-like metalloenzymes, cyanobacterial halogenases, radical-initiating metallocofactors, and iron-dependent oxygenases, contributing to the understanding of enzyme mechanisms and biosynthesis pathways.
Research topics
- Chemistry
- Biochemistry
- Stereochemistry
- Biology
- Internal medicine
- Photochemistry
- Medicinal chemistry
- Organic chemistry
- Virology
Selected publications
Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets
Science · 2021 · 126 citations
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causal agent of COVID-19, uses an RNA-dependent RNA polymerase (RdRp) for the replication of its genome and the transcription of its genes. We found that the catalytic subunit of the RdRp, nsp12, ligates two iron-sulfur metal cofactors in sites that were modeled as zinc centers in the available cryo-electron microscopy structures of the RdRp complex. These metal binding sites are essential for replication and for interaction with…
Journal of the American Chemical Society · 2020 · 81 citations
xidases and oxygenases (HDOs).
Nature Communications · 2020 · 71 citations
] cluster acquisition and coordination. The enzymatic activity of human ALAD is greatly reduced upon loss of its Fe-S cluster, which results in reduced heme biosynthesis in human cells. As ALAD provides an early Fe-S-dependent checkpoint in the heme biosynthetic pathway, our findings help explain why heme biosynthesis depends on intact ISC biogenesis.
Proceedings of the National Academy of Sciences · 2023-08-08 · 47 citations
articleOpen accessSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19, uses an RNA-dependent RNA polymerase along with several accessory factors to replicate its genome and transcribe its genes. Nonstructural protein (nsp) 13 is a helicase required for viral replication. Here, we found that nsp13 ligates iron, in addition to zinc, when purified anoxically. Using inductively coupled plasma mass spectrometry, UV-visible absorption, EPR, and Mössbauer spectroscopies, we char…
Journal of the American Chemical Society · 2021 · 47 citations
]-l-Arg slows decay of the ferryl complex by >16-fold, implying that RO is initiated by hydrogen-atom transfer (HAT) from C5. That this large substrate deuterium kinetic isotope effect has no impact on the EF:RO partition ratio implies that the same ferryl intermediate cannot be on the EF pathway; the pathways must diverge earlier. Consistent with this conclusion, the variant enzyme bearing the Asp191Glu ligand substitution accumulates ∼4 times as much of the ferryl complex as the wild-type enzy…
Recent grants
NIH · $1.1M · 2011
Mechanisms and Reprogramming of Iron/2-Oxoglutarate Desaturases and Oxacyclases
NIH · $1.0M · 2016–2021
NIH · $3.7M · 2013
Frequent coauthors
- 211 shared
Carsten Krebs
Pennsylvania State University
- 64 shared
Boi Hanh Huynh
- 59 shared
Eric W. Barr
University of Pennsylvania
- 55 shared
Lana Saleh
- 52 shared
Christopher T. Walsh
Met Office
- 46 shared
Jeffrey Baldwin
The University of Texas Southwestern Medical Center
- 44 shared
Edward I. Solomon
SLAC National Accelerator Laboratory
- 43 shared
Brenda A. Ley
Pennsylvania State University
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