page_title: William B. Tolman
section_title: Copper-Oxygen Adducts
hierarchical_section_title: William B. Tolman / Copper-Oxygen Adducts
caption_attribution_description: English: This figure shows copper and oxygen bonded at differing ratios.
context_page_description: William B. Tolman is an inorganic chemist whose laboratory works on synthesis and characterization of bioinorganic systems, organometallic reagents and polymers. He received his bachelor's degree in Chemistry from Wesleyan University in 1983, and then completed a Ph.D. program in Chemistry at the University of California, Berkeley by 1987 under the guidance of Professor K. Peter C. Vollhardt. He previously was employed at the University of Minnesota as the Department Chair of Chemistry. Currently, he is the William Greenleaf Eliot Professor of Chemistry at Washington University in St. Louis. In addition to his faculty position, he is also the Editor and Chief of the ACS journal of Inorganic Chemistry.
context_section_description: Tolman's work in the bioinorganic field focuses on Cu-O adducts, specifically copper proteins whose diverse, biological functions include: O₂ transport, aromatic ring oxidations, biogenesis of hormones.  His work studies the potential of 1:1 Cu/O₂ adducts as catalytic species, which have been known as transient intermediates for more commonly studied 2:1 and even 3:1 Cu/O₂ molecules. These complexes, while kinetically favored in formation are thermodynamically unstable due to negative entropy values, thus making them more difficult to isolate. Although, increasing ligand sizes on these 1:1 adducts did correlate with slower reaction rate constants; advantageous for isolating and studying these complexes.
  Furthermore, his work on high and mixed valent copper species including [CuOH]⁺² and its conjugate base, [CuO]⁺ is also very notable. His work with [CuOH]+2 reveals a high reactivity with C-H and O-H bonds as compared to its conjugate acid pair. This is of importance when trying to replicate biological mechanisms, such as copper-catalyzed oxidation in vitro.
  His research has greatly contributed to the discovery and characterization of new biomimetic species. It is his goal to not only identify these compounds, but to comprehensively understand the intermediates and mechanisms with which they play crucial roles in facilitating. In the case of Cu/O₂ adducts, realizing their biological role and function in copper containing enzymes can give rise to new insights on their biomimetic properties.
  Additionally, his lab is searching for alternative, synthetic oxidative catalysis. This includes designing biochemically-inspired synthetic catalysts as well as trying O₂ as a candidate for controlled, in vitro oxidation. Due to high abundances and relatively strong stabilizing capabilities within biological reactions, iron and copper enzymes inspire biomimetic synthetic catalysts. Although these reactions perform with high accuracy and selectivity within the body, many challenges arise when working with O2 in vitro because of the undesired and potentially harmful side products that can be generated.
caption: This figure shows copper and oxygen bonded at differing ratios.
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