David Goldberg

About

Dr. David Goldberg's research focuses on employing synthetic inorganic chemistry to answer fundamental questions regarding structure, spectroscopy, and reactivity pertinent to bioinorganic chemistry. His work involves understanding how transition metal ions in enzymes catalyze critical reactions related to energy utilization, biosynthetic pathways, natural defense systems, and cell signaling. The Goldberg laboratory aims to determine the fundamental principles that control this chemistry, including the key bond-making and bond-breaking steps at the metal center that enable these reactions. His research includes the synthesis of novel mononuclear Fe and Mn complexes that mimic features of both heme- and non-heme metal centers in biology, such as high-valent metal-oxo and metal-peroxo complexes relevant to oxygenases and other metalloenzymes. The lab employs ligand design and organic chemistry tools to tune the coordination sphere around the metal center, controlling reactivity and establishing structure-function relationships. Techniques such as inorganic spectroscopic methods—including EPR, Mössbauer, resonance Raman, and X-ray absorption spectroscopies—are integral to his work, often in collaboration with experts. Computational studies, including DFT, are routinely used to guide and inform the research.

Research topics

• Photochemistry
• Medicinal chemistry
• Chemistry
• Organic chemistry
• Stereochemistry
• Computational chemistry

Selected publications

• What Drives Radical Halogenation versus Hydroxylation in Mononuclear Nonheme Iron Complexes? A Combined Experimental and Computational Study

  Journal of the American Chemical Society · 2022 · 61 citations

  transfer with tertiary radicals. Comprehensive computational studies involving density functional theory were carried out to examine the possible origins of this selectivity. The calculations reproduce the experimental findings, which indicate that halogen transfer is not observed for the tertiary radicals because of a nonproductive equilibrium that results from the endergonic nature of these reactions, despite a potentially lower reaction barrier for the halogenation pathway. In contrast, halog…

  DOI

• Determining the Inherent Selectivity for Carbon Radical Hydroxylation versus Halogenation with Fe^III(OH)(X) Complexes: Relevance to the Rebound Step in Non-heme Iron Halogenases

  Journal of the American Chemical Society · 2020 · 45 citations

  Senior authorCorresponding

  complex reacts with carbon radicals to give halogenation. These results are discussed in terms of the inherent reactivity of the analogous rebound intermediate in both enzymes and related catalysts.

  DOI

• Hydroxyl Transfer to Carbon Radicals by Mn(OH) vs Fe(OH) Corrole Complexes

  Inorganic Chemistry · 2020 · 29 citations

  Senior authorCorresponding

  C• (X = tBu, CN) also give good linear correlations, and a comparison of the resulting activation parameters highlight the importance of entropy in these •OH transfer reactions. Density functional theory calculations of the reaction profiles show a concerted process with one transition state for all radicals investigated and help to explain the electronic features of the OH rebound process.

  DOI

• Chemoselective Proteomics, Zinc Fingers, and a Zinc(II) Model for H₂S Mediated Persulfidation

  Angewandte Chemie International Edition · 2024-05-29 · 19 citations

  articleOpen accessCorresponding

  Abstract The gasotransmitter hydrogen sulfide (H 2 S) is thought to be involved in the post‐translational modification of cysteine residues to produce reactive persulfides. A persulfide‐specific chemoselective proteomics approach with mammalian cells has identified a broad range of zinc finger (ZF) proteins as targets of persulfidation. Parallel studies with isolated ZFs show that persulfidation is mediated by Zn II , O 2 , and H 2 S, with intermediates involving oxygen‐ and sulfur‐based radical…

  PublisherOA PDFDOI

• A Nonheme Iron(III) Superoxide Complex Leads to Sulfur Oxygenation

  Journal of the American Chemical Society · 2024-03-15 · 18 citations

  articleOpen accessSenior authorCorresponding

  A new alkylthiolate-ligated nonheme iron complex, FeII(BNPAMe2S)Br (1), is reported. Reaction of 1 with O2 at −40 °C, or reaction of the ferric form with O2•– at −80 °C, gives a rare iron(III)-superoxide intermediate, [FeIII(O2)(BNPAMe2S)]+ (2), characterized by UV–vis, 57Fe Mössbauer, ATR-FTIR, EPR, and CSIMS. Metastable 2 then converts to an S-oxygenated FeII(sulfinate) product via a sequential O atom transfer mechanism involving an iron-sulfenate intermediate. These results provide evidence f…

  PublisherOA PDFDOI

Recent grants

• New Vistas in Porphyrinoid Chemistry: Corrolazine Synthesis and Reactivity

  NSF · $400k · 2006–2009

• New Vistas in Porphyrinoid Chemistry: Corrolazine Synthesis and Reactivity

  NSF · $170k · 2012–2013

• Synthetic Nonheme Iron O2 Activation and S-Oxygenation

  NIH · $3.2M · 2016–2025

Frequent coauthors

• Maxime A. Siegler

  163 shared

• Joshua Telser

  Roosevelt University

  97 shared

• Arnold L. Rheingold

  University of California, San Diego

  89 shared

• J. Krzystek

  National High Magnetic Field Laboratory

  80 shared

• Bobby Ramdhanie

  Johns Hopkins University

  78 shared

• Lev N. Zakharov

  Oregon State University

  63 shared

• Pierre Moënne‐Loccoz

  Oregon Health & Science University

  56 shared

• Brian M. Hoffman

  Northwestern University

  52 shared

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