Dennis R. Dean

About

Dennis R. Dean is a University Distinguished Professor in the Department of Biochemistry at Virginia Tech, with his research focused on the biochemistry of biological nitrogen fixation and the biological pathways for assembly of simple and complex metalloclusters. His laboratory has developed biochemical-genetic approaches to identify substrate interactions with nitrogenase, leading to a comprehensive model of substrate interaction at the nitrogenase active site. Recently, in collaboration with Lance Seefeldt, his team used genetic approaches to remodel nitrogenase, enabling it to reduce carbon dioxide to produce methane and short-chain olefins, which suggests potential avenues for metal-based catalysts in carbon dioxide sequestration. His research also investigates the biological assembly of iron-sulfur clusters, which are among nature’s most ancient prosthetic groups and may have contributed to the emergence of life on earth. His group discovered the biological mechanism for iron-sulfur cluster assembly and introduced the concept that these prosthetic groups are pre-assembled on molecular scaffolds. Both in vitro and in vivo approaches have established the universality of these processes, with ongoing work including structural elucidation of biosynthetic complexes and whole-genome transcriptome analysis of bacterial strains defective in iron-sulfur assembly. Dr. Dean has held various leadership roles, including Director of the Fralin Life Science Institute since 2008, and…

Research topics

• Chemistry
• Photochemistry
• Organic chemistry
• Biochemical engineering
• Stereochemistry
• Ecology
• Crystallography
• Medicinal chemistry
• Combinatorial chemistry
• Inorganic chemistry

Selected publications

• Reduction of Substrates by Nitrogenases

  Chemical Reviews · 2020 · 389 citations

  , is also discussed, and remaining challenges in understanding nitrogenase substrate reduction are considered.

  DOI

• Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in <i>Azotobacter vinelandii</i>

  Critical Reviews in Biochemistry and Molecular Biology · 2022-11-02 · 47 citations

  reviewOpen accessCorresponding

  Understanding how Nature accomplishes the reduction of inert nitrogen gas to form metabolically tractable ammonia at ambient temperature and pressure has challenged scientists for more than a century. Such an understanding is a key aspect toward accomplishing the transfer of the genetic determinants of biological nitrogen fixation to crop plants as well as for the development of improved synthetic catalysts based on the biological mechanism. Over the past 30 years, the free-living nitrogen-fixin…

  PublisherOA PDFDOI

• Comment on “Structural evidence for a dynamic metallocofactor during N ₂ reduction by Mo-nitrogenase”

  Science · 2021-02-11 · 40 citations

  letterOpen access

  Kang et al . (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N 2 or an N 2 -derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.

  PublisherOA PDFDOI

• Electron Redistribution within the Nitrogenase Active Site FeMo-Cofactor During Reductive Elimination of H₂ to Achieve N≡N Triple-Bond Activation

  Journal of the American Chemical Society · 2020 · 40 citations

  Fe signals are suggested as associated with structurally identified "anchors" of one bridging hydride, two others with identified anchors of the second, with NBO-analysis further identifying one anchor of each hydride as a major recipient of electrons released upon breaking Fe-H bonds.

  PublisherOA PDFDOI

• The electronic structure of FeV-cofactor in vanadium-dependent nitrogenase

  Chemical Science · 2021-01-01 · 32 citations

  articleOpen accessCorresponding

  Active site FeV-cofactor of the V-nitrogenase and the EPR spectrum of the reduced cofactor showing ⁵¹V-hyperfine coupling.

  PublisherDOI

Recent grants

• Iron-sulfur Cluster Assembly in Bacteria

  NSF · $624k · 2002–2007

• Maturation of [Fe-S] Proteins in Bacteria

  NSF · $820k · 2007–2013

Frequent coauthors

• Lance C. Seefeldt

  301 shared

• Brian M. Hoffman

  Northwestern University

  271 shared

• Mikhail Laryukhin

  National Eye Institute

  132 shared

• Hong-In Lee

  Kyungpook National University

  126 shared

• Patricia C. Dos Santos

  Wake Forest University

  115 shared

• Robert Y. Igarashi

  University of Central Florida

  103 shared

• Tran-Chin Yang

  Northwestern University

  75 shared

• Brett M. Barney

  University of Minnesota

  74 shared

Labs

• Dennis R. Dean LaboratoryPI

Education

• Doctor of Philosophy, Molecular Biology

  Purdue University

  1979

• Bachelor of Arts

  Wabash College

  1973

Similar researchers at Virginia Tech

• Richard Helmh-48
• Michael Klembah-29
• Chloe Lahondereh-20