Bio


Professor Emeritus James Collman has made landmark contributions to inorganic chemistry, metal ion biochemistry, homogeneous catalysis, and transition metal organometallic chemistry. He pioneered numerous now-popular research tools to reveal key structural and functional details of metalloenzymes essential to respiration and energy, and hemoglobin and myoglobin, essential to oxygen transport in the blood.

Born 1932 in Beatrice, Nebraska, James P. Collman studied chemistry at U. Nebraska–Lincoln (B.S. 1954, M.S. 1956). His doctoral work at U. Illinois at Urbana-Champaign (Ph.D., 1958) focused on Grignard reagents. As a faculty member at U. North Carolina, he demonstrated aromatic reactivity in metal acetylacetonates, and he developed metal complexes that hydrolyze peptide bonds under physiological conditions. He came to Stanford University as Professor of Chemistry in 1967. Among many honors, Prof. Collman’s was elected to the National academy of Sciences in 1975, and named California Scientist of the Year in 1983.

At Stanford, Prof. Collman invented a new paradigm for studying biological systems using functional synthetic analogs of metal-containing enzyme systems, free from the protein coatings that can affect metalloprotein chemical properties. This strategy allowed him to elucidate the intrinsic reactivity of the metal center as well as the effects of protein-metal interactions on biological function.

One focal point of this research has involved heme-proteins such as the oxygen (O2) carrier hemoglobin (Hb), and the O2-storing protein myoglobin (Mb). Prof. Collman was the first to prepare and characterize stable, functional analogues of the Hb and Mb active sites, which contain an iron derivative of the large flat “porphyrin” ligand. In his “picket fence” porphyrin, groups installed on the periphery block side reactions, which would otherwise degrade the structure. This protected iron complex manifests the unique magnetic, spectroscopic and structural characteristics of the O2-binding Hb and Mb sites, and exhibits very similar O2-binding affinities.

The Collman Group also prepared functional mimics of the O2-binding/reducing site in a key respiration enzyme, cytochrome c oxidase, CcO, which converts O2 to H2O during biosynthesis of the energy storage molecule ATP. This enzyme must be very selective: partial O2 reduction products are toxic. Prof. Collman invented a powerful synthetic strategy to create analogs of the CcO active site and applied novel electrochemical techniques to demonstrate that these models catalyze the reduction of O2 to water without producing toxic partially-reduced species. He was able to mimic slow, rate-limiting electron delivery by attaching his CcO model to a liquid-crystalline membrane using “click chemistry.” He demonstrated that hydrogen sulfide molecules and heterocycles reversibly bind to the metal centers at CcO’s active site, connecting a synthetic enzyme model to simple molecules that reversibly inhibit respiration. These respiration inhibitors exhibit physiological properties, affecting blood clotting and controlling the effects of the hormone, nitric oxide, NO.

In addition, Prof. Collman performed fundamental studies of organometallic reactions. He also prepared and characterized homodinuclear and heterodinuclear complexes having metal-metal multiple bonds, and made the first measurements of the rotational barriers found in multiple metal-metal bonds.

Prof. Collman’s impactful textbook “Principles and Applications of Organotransition Metal Chemistry” has seen multiple editions. His book “Naturally Dangerous: Surprising Facts About Food, Health, and the Environment” explains the science behind everyday life, and received favorable reviews in Nature and The Washington Post.

Academic Appointments


Administrative Appointments


  • Professor of Chemistry, Stanford University (1967 - Present)
  • Professor of Organic and Inorganic Chemistry, University of North Carolina (1966 - 1967)
  • Associate Professor, University of North Carolina (1962 - 1962)
  • Assistant Professor, University of North Carolina (1959 - 1962)
  • Instructor, University of North Carolina (1958 - 1959)

Honors & Awards


  • Ronald Breslow Award for Achievement in Biomimetic Chemistry, American Chemical Society (2009)
  • Alfred Bader Award in Bioinorganic or Bioorganic Chemistry, American Chemical Society (1997)
  • Pauling Award, American Chemical Society, Puget Sound and Oregon Section (1990)
  • Honorary Doctorate, University of Nebraska (1988)
  • Docteur Honoris Causa, Universite de Bourgogne, France (1988)
  • California Scientist of the Year Award, California Science Center (1983)
  • Member, American Academy of Arts and Sciences (1975)
  • Member, National Academy of Sciences (1975)
  • Award in Inorganic Chemistry, American Chemical Society (1975)
  • ACS California Section Award (13 Western States), American Chemical Society (1972)
  • International Award in Coordination Chemistry, Japanese Society of Coordination Chemistry (2008)
  • The Oesper Award, Cincinnati Section of the American Chemical Society (2007)
  • Fellow, American Association for the Advancement of Science (2004)
  • Hans Fischer Award in Porphyrin Chemistry, International Conference of Porphyrins and Phthalocyanines, Japan (2002)
  • Basolo Medal, American Chemical Society (2000)
  • Joseph Chatt Lectureship, Royal Society of Chemistry (1998)
  • John C. Bailar Jr. Medal, University of Illinois, Urbana-Champaign (1995)
  • Award for Distinguished Service in the Advancement of Inorganic Chemistry, American Chemical Society (1991)
  • Arthur C. Cope Scholar Award, American Chemical Society (1986)
  • Guggenheim Fellow, John Simon Guggenheim Foundation (1985-86)
  • Guggenheim Fellow, John Simon Guggenheim Foundation (1977-78)

Boards, Advisory Committees, Professional Organizations


  • Member, Stanford Department of Chemistry Industrial Affiliates Committee
  • Member, Stanford Department of Chemistry Executive Committee
  • Member, Stanford Department of Chemistry Graduate Admissions Committee

Professional Education


  • PhD, University of Illinois at Urbana-Champaign, Organic Chemistry (1958)
  • MS, University of Nebraska, Inorganic Chemistry (1956)
  • BS, University of Nebraska, Chemistry (1954)

All Publications


  • Inhibiting platelet-stimulated blood coagulation by inhibition of mitochondrial respiration PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Barile, C. J., Herrmann, P. C., Tyvoll, D. A., Collman, J. P., Decreau, R. A., Bull, B. S. 2012; 109 (7): 2539-2543

    Abstract

    Platelets are important mediators of blood coagulation that lack nuclei, but contain mitochondria. Although the presence of mitochondria in platelets has long been recognized, platelet mitochondrial function remains largely unaddressed. On the basis of a small amount of literature that suggests platelet mitochondria are functional, we hypothesized that the inhibition of platelet mitochondria disrupts platelet function and platelet-activated blood coagulation. To test this hypothesis, members of the tetrazole, thiazole, and 1,2,3-triazole families of small molecule heterocycles were screened for the ability to inhibit isolated mitochondrial respiration and coagulation of whole blood. The families of heterocycles screened were chosen on the basis of the ability of the heterocycle family to inhibit a biomimetic model of cytochrome c oxidase (CcO). The strength of mitochondrial inhibition correlates with each compound's ability to deter platelet stimulation and platelet-activated blood clotting. These results suggest that for this class of molecules, inhibition of blood coagulation may be occurring through a mechanism involving mitochondrial inhibition.

    View details for DOI 10.1073/pnas.1120645109

    View details for Web of Science ID 000300489200075

    View details for PubMedID 22308457

    View details for PubMedCentralID PMC3289322

  • Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Collman, J. P., Ghosh, S., Dey, A., Decreau, R. A. 2009; 106 (52): 22090-22095

    Abstract

    The toxic gas H(2)S is produced by enzymes in the body. At moderate concentrations, H(2)S elicits physiological effects similar to hibernation. Herein, we describe experiments that imply that the phenomenon probably results from reversible inhibition of the enzyme cytochrome c oxidase (CcO), which reduces oxygen during respiration. A functional model of the oxygen-reducing site in CcO was used to explore the effects of H(2)S during respiration. Spectroscopic analyses showed that the model binds two molecules of H2S. The electro-catalytic reduction of oxygen is reversibly inhibited by H(2)S concentrations similar to those that induce hibernation. This phenomenon derives from a weak, reversible binding of H(2)S to the Fe(II) porphyrin, which mimics heme a(3) in CcO's active site. No inhibition of CcO is detected at lower H(2)S concentrations. Nevertheless, at lower concentrations, H(2)S could have other biological effects on CcO. For example, H(2)S rapidly reduces Fe(III) and Cu(II) in both the oxidized form of this functional model and in CcO itself. H(2)S also reduces CcO's biological reductant, cytochrome c, which normally derives its reducing equivalents from food metabolism. Consequently, it is speculated that H(2)S might also serve as a source of electrons during periods of hibernation when food supplies are low.

    View details for DOI 10.1073/pnas.0904082106

    View details for Web of Science ID 000273178700012

    View details for PubMedID 20007376

    View details for PubMedCentralID PMC2799705

  • Functional biomimetic models for the active site in the respiratory enzyme cytochrome c oxidase CHEMICAL COMMUNICATIONS Collman, J. P., Decreau, R. A. 2008: 5065-5076

    Abstract

    A functional analog of the active site in the respiratory enzyme, cytochrome c oxidase (CcO) reproduces every feature in CcO's active site: a myoglobin-like heme (heme a3), a distal tridentate imidazole copper complex (Cu(B)), a phenol (Tyr244), and a proximal imidazole. When covalently attached to a liquid-crystalline SAM film on an Au electrode, this functional model continuously catalyzes the selective four-electron reduction of dioxygen at physiological potential and pH, under rate-limiting electron flux (as occurs in CcO).

    View details for DOI 10.1039/b808070b

    View details for Web of Science ID 000260407400001

    View details for PubMedID 18956030

  • A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux SCIENCE Collman, J. P., Devaraj, N. K., Decreau, R. A., Yang, Y., Yan, Y., Ebina, W., Eberspacher, T. A., Chidsey, C. E. 2007; 315 (5818): 1565-1568

    Abstract

    We studied the selectivity of a functional model of cytochrome c oxidase's active site that mimics the coordination environment and relative locations of Fe(a3), Cu(B), and Tyr(244). To control electron flux, we covalently attached this model and analogs lacking copper and phenol onto self-assembled monolayer-coated gold electrodes. When the electron transfer rate was made rate limiting, both copper and phenol were required to enhance selective reduction of oxygen to water. This finding supports the hypothesis that, during steady-state turnover, the primary role of these redox centers is to rapidly provide all the electrons needed to reduce oxygen by four electrons, thus preventing the release of toxic partially reduced oxygen species.

    View details for DOI 10.1126/science.1135844

    View details for Web of Science ID 000244934800049

    View details for PubMedID 17363671

    View details for PubMedCentralID PMC3064436

  • The first quadruple bond between elements of different groups ANGEWANDTE CHEMIE-INTERNATIONAL EDITION Collman, J. P., Boulatov, R., Jameson, G. B. 2001; 40 (7): 1271-?
  • O-2 AND CO BINDING TO IRON(II) PORPHYRINS - A COMPARISON OF THE PICKET FENCE AND POCKET PORPHYRINS JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Collman, J. P., Brauman, J. I., Iverson, B. L., Sessler, J. L., Morris, R. M., Gibson, Q. H. 1983; 105 (10): 3052-3064
  • COOPERATIVITY IN O-2 BINDING TO IRON PORPHYRINS PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Collman, J. P., Brauman, J. I., Rose, E., Suslick, K. S. 1978; 75 (3): 1052-1055

    Abstract

    The solid-gas O2 binding equilibrium has been studied for for ferrous "picket fence" porphyrinates with sterically hindered axial imidazoles. Such systems show significant cooperativity in their binding of O2: at low O2 pressures a low O2 affinity form exists, and at high O2 pressures a higher O2 affinity form develops. Direct analogies are drawn to the cooperativity shown in O2 binding by hemoglobin. These model systems mimic hemoglobin quantitatively.

    View details for Web of Science ID A1978EU94600003

    View details for PubMedID 274696

  • MODEL COMPOUNDS FOR T-STATE OF HEMOGLOBIN PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Collman, J. P., Brauman, J. I., Doxsee, K. M., HALBERT, T. R., Suslick, K. S. 1978; 75 (2): 564-568

    Abstract

    O2 binding to a series of ferrous and cobaltous "picket fence" porphyrins is reported. N-Methylimidazole and covalently attached imidazoles gives O2 binding to ferrous porphyrins with deltaH degrees =-16.2 kcal/mol (-67.7 kJ/mol) and deltaS degrees =-40 eu (standard state, 1 atmosphere O2). Similar studies with cobaltous porphyrins yield deltaH degrees =- 12.8 kcal/mol (-53.5 kJ/mol) and deltaS degrees =- 39 eu. These values match well those of myoglobin and isolated subunits of hemoglobin and their cobalt reconstituted analogues. 1,2-Dimethylimidazole has been successfully used to mimic the presumed restraint of T state hemoglobin. In direct analogy to the decreased cooperativity shown by cobalt-substituted hemoglobin, model cobalt porphyrins show a smaller decrease in O2 affinity than the analogous iron porphyrins when the axial base is hindered. Thermodynamic data are presented. The molecular mechanism of cooperativity in hemoglobin is discussed.

    View details for Web of Science ID A1978EQ77900007

    View details for PubMedID 273219

  • PICKET-FENCE PORPHYRINS - SYNTHETIC MODELS FOR OXYGEN BINDING HEMOPROTEINS JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Collman, J. P., GAGNE, R. R., Reed, C. A., HALBERT, T. R., Lang, G., Robinson, W. T. 1975; 97 (6): 1427-1439

    View details for Web of Science ID A1975V896700026

    View details for PubMedID 1133392

  • REVERSIBLE OXYGEN ADDUCT FORMATION IN FERROUS COMPLEXES DERIVED FROM A PICKET FENCE PORPHYRIN - MODEL FOR OXYMYOGLOBIN JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Collman, J. P., GAGNE, R. R., HALBERT, T. R., Marchon, J. C., Reed, C. A. 1973; 95 (23): 7868-7870

    View details for Web of Science ID A1973R263300054

    View details for PubMedID 4759037