J
Joan B. Broderick
Researcher at Montana State University
Publications - 121
Citations - 6813
Joan B. Broderick is an academic researcher from Montana State University. The author has contributed to research in topics: Radical SAM & Hydrogenase. The author has an hindex of 44, co-authored 107 publications receiving 5953 citations. Previous affiliations of Joan B. Broderick include University of Georgia & Lawrence Berkeley National Laboratory.
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Radical S-Adenosylmethionine Enzymes
TL;DR: This Review will begin by summarizing unifying features of radical SAM enzymes, and in subsequent sections delve further into the biochemical, spectroscopic, structural, and mechanistic details for those enzymes that catalyze an amazingly diverse set of reactions.
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[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation
John W. Peters,Gerrit J. Schut,Eric S. Boyd,David W. Mulder,Eric M. Shepard,Joan B. Broderick,Paul W. King,Michael W. W. Adams +7 more
TL;DR: These mechanisms represent two independent solutions to the formation of complex bioinorganic active sites for catalyzing the simplest of chemical reactions, reversible hydrogen oxidation, and are arguably the most profound case of convergent evolution.
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Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG).
David W. Mulder,Eric S. Boyd,Ranjana Sarma,Rachel K. Lange,James A. Endrizzi,Joan B. Broderick,John W. Peters +6 more
TL;DR: In this article, the X-ray crystal structure of Chlamydomonas reinhardtii HydA was solved, revealing the stepwise manner by which the H-cluster is synthesized, and offering insight into how HydA might have evolved.
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Insights into [FeFe]-Hydrogenase Structure, Mechanism, and Maturation
David W. Mulder,Eric M. Shepard,Jonathan E. Meuser,Neelambari Joshi,Paul W. King,Matthew C. Posewitz,Joan B. Broderick,John W. Peters +7 more
TL;DR: This review highlights the unique structural features of hydrogenases and emphasizes the recent biochemical and structural work that has created a clearer picture of the [FeFe]-hydrogenase maturation pathway.
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Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
Jessica L. Vey,Jian Yang,Meng Li,William E. Broderick,Joan B. Broderick,Catherine L. Drennan +5 more
TL;DR: Structures of the substrate-free and substrate-bound forms of pyruvate formate-lyase-activating enzyme, the first structures of an AdoMet radical activase, are reported, providing fundamental insights into the interactions between the activase and the G734 loop ofPyruvates.