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We determine the catalytic mechanisms of metalloenzymes through the development and implementation of electron-nuclear double resonance (ENDOR) spectroscopy, a combination of NMR and EPR. This technique is uniquely able to determine active site composition, electronic and geometric structures, not merely for the resting state but, most importantly, for key trapped catlalytic intermediates. This approach is applied to complex multi-metallic catalytic centers, as in the globally important enzyme, nitrogenase, which provides nitrogen as nutrient for most of the planet, as well as to key mononuclear centers, as in the physiologically vital heme enzymes nitric oxide synthase and cytochrome P450. In parallel, we study biomimetic complexes that provide constraints that help identify intermediates trapped during catalysis, and that are moreover of intrinsic importance as Jahn-Teller active systems whose H2 complexes exhibit novel dynamic properties. A second area of research is the study of long-range electron transfer between proteins. We focus on the central question: how do conformational dynamics at a protein-protein interface control inter-protein electron transfer? As protein-protein interactions are central to almost all biological processes, this focus links our research to other major problems in biology.
We determine the catalytic mechanisms of metalloenzymes through the development and implementation of electron-nuclear double resonance (ENDOR) spectroscopy, a combination of NMR and EPR. This technique is uniquely able to determine active site composition, electronic and geometric structures, not merely for the resting state but, most importantly, for key trapped catlalytic intermediates. This approach is applied to complex multi-metallic catalytic centers, as in the globally important enzyme, nitrogenase, which provides nitrogen as nutrient for most of the planet, as well as to key mononuclear centers, as in the physiologically vital heme enzymes nitric oxide synthase and cytochrome P450. In parallel, we study biomimetic complexes that provide constraints that help identify intermediates trapped during catalysis, and that are moreover of intrinsic importance as Jahn-Teller active systems whose H2 complexes exhibit novel dynamic properties. A second area of research is the study of long-range electron transfer between proteins. We focus on the central question: how do conformational dynamics at a protein-protein interface control inter-protein electron transfer? As protein-protein interactions are central to almost all biological processes, this focus links our research to other major problems in biology.
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Journal of the American Chemical Societyno. 6 (2024): 3710-3720
JOURNAL OF THE AMERICAN CHEMICAL SOCIETYno. 6 (2024): 3710-3720
Selamawit Ghebreamlak,Sebastian A Stoian,Nicholas S Lees,Bryan Cronin,Forrest Smith,Matthew O Ross,Joshua Telser,Brian M Hoffman,Evert C Duin
Journal of the American Chemical Societyno. 6 (2024): 3926-3942
Nature Chemistryno. 5 (2023): 658-665
JOURNAL OF BIOLOGICAL CHEMISTRYno. 3 (2023): S302-S302
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICAno. 47 (2023): e2314696120-e2314696120
Fatima Abi Ghaida, Katharina Brinkert,Ping Chen,Serena DeBeer,Brian M Hoffman,Patrick L Holland,Shoba Laxmi,Doug MacFarlane,Jonas C Peters,John W Peters, Christopher J Pickett,Lance C Seefeldt,
Faraday discussions (2023)
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Nature catalysisno. 12 (2023): 1194-1204
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