Santa Clara University

bioengineering

James P. Collman

collman
 
Ph.D., George A. and Hilda M. Daubert Professor, Department of Chemistry, Stanford University

Education

B.S., 1954, University of Nebraska;
M.S., 1956;
Ph.D., 1958, University of Illinois

Awards

ACS Award in Inorganic Chemistry, 1975; National Academy of Sciences, 1975; American Academy of Arts and Sciences, 1975; Guggenheim Fellow, 1977-78 and 1985-86; California Scientist of the Year Award, 1983; ACS Arthur C. Cope Scholar Award, 1986; ACS (Puget Sound and Oregon Section) Pauling Award, 1990; ACS Award for Distinguished Service in the Advancement of Inorganic Chemistry, 1991; John C. Bailar Jr., Medalist, 1995; ACS Alfred Bader Award in Bioinorganic or Bioorganic Chemistry, 1997; Joseph Chatt Lectureship, 1998; Basolo Medal, Chicago, American Chemical Society, October 6, 2000; Hans Fischer Award in Porphyrin Chemistry, International Conference of Porphyrins and Phthalocyanines, Japan, 2002; Fellow, American Association for the Advancement of Science, 2004; The Oesper Award, 2007; International Award in Coordination Chemistry from the Japanese Society of Coordination Chemistry, 2008; Ronald Breslow Award for Achievement in Biomimetic Chemistry, American Chemical Society, 2009.

Chemistry Research Area

Inorganic
Organic
Organometallic

Principal Research Interests

The catalysis of multi-electron redox reactions is a fundamental problem that has been solved in certain biological systems through the agency of multimetallic enzymes (cytochrome c oxidase, laccase, and nitrogenase). The detailed mechanisms by which these metalloenzymes function are still obscure. Our research is directed towards the synthesis of functional biomimetic catalysts for the electrochemical reduction of dioxygen to water (a 4e- process), nitrogen to ammonia (a 6e- process), and the oxidation of hydrogen (a 2e- process). Recently we have developed several functional models for the active site in cytochrome c oxidase. These complexes reduce O2 by 4e- at pH. Our complex that is structurally closest to "the real thing," is the best catalyst. By studying the electrocatalytic reduction of dioxgen in lipid layers under conditions of slow electron delivery, we have shown that Cub and an appended tyrosine (Try-244) is necessary to afford selective 4e reduction of dioxygen at physiological potentials. By using our functional model we are exploring the action of hydrogen sulfide interacting with cytochrome c oxidase. Hydrogen sulfide can produce a state of hibernation in animals, probably by its interaction with cytochrome c oxidase. Understanding this process could lead to drugs that induce hypoxia and may have many medical applications.

Representative Publications

(1) "Inhibiting platelet-stimulated blood coagulation by inhibition of mitochondrial respiration," C.J. Barile, P.C. Herrmann, D.A. Tyvoll, J.P. Collman, R.A. Decreau, B.S. Bull, Natl. Acad. Sci. USA, 109, 2539-2543 (2012).

(2) "Role of a Distal Pocket in the Catalytic O2 Reduction by Cytochrome c Oxidase Models Immobilized on Interdigitated Array Electrodes," J.P. Collman, R.A. Decreau, H. Lin, A. Hosseini, Y. Yang, A. Dey, T.A. Eberspacher, Proc. Natl. Acad. Sci. U.S A, Early Edition, (2009).

(3) "Catalytic Reduction of O2 by Cytochrome c Using a Synthetic Model of Cytochrome c Oxidase," J.P. Collman, S. Ghosh, A. Dey, R.A. Decreau, Y. Yang, J. Am. Chem. Soc., 131, 5034-5035 (2009).

(4) "A Functional Nitric Oxide Reductase Model," J.P. Collman, Y. Yang, A. Dey, R.A. Decreau, S. Ghosh, T. Otah, E.I. Solomon, Proc. Natl. Acad. Sci. U. S. A., 105, 15660-15665 (2008).

(5) "Functional Biomimetic Models for the Active Site in the Respiratory Enzyme Cytochrome c oxidase," J.P. Collman, R.A. Decréau, Chem. Comm, 5065-5076 (2008).

(6) "Interaction of nitric oxide with a functional model of cytochrome c oxidase," J.P. Collman, A. Dey, R.A. Decreau, Y. Yang, A. Hosseini, E.I. Solomon, T.A. Eberspacher, Proc. Natl. Acad. Sci. U. S. A, 155, 9892-9896 (2008).

(7) "Single-Turnover Reaction in a Cytochrome c Oxidase Model Bearing a Tyr244 Mimic," R.A. Decreau, J.P. Collman, Y. Yan, J. Yoon, E.I. Solomon, J. Am. Chem. Soc., 129, 5794 - 5795 (2007).

(8) "A Cytochrome c Oxidase Model Catalyzes Oxygen to Water Reduction Under Rate-Limiting Electron Flux," J.P. Collman, N.K. Devaraj, R.A. Decreau, Y. Yang, Y. Yan, W.Ebina, T.A. Eberspacher, C.E.D. Chidsey, Science, 315, 1565-1568 (2007).

(9) "Active-Site Models of Bacterial Nitric Oxide Reductase Featuring Tris-Histidyl and Glutamic Acid Mimics: Influence of a Carboxylate Ligand on FeB Binding and the Heme Fe/FeB Redox Potential," J.P. Collman, Y. Yan, J. Lei, P.H. Dinolfo, Inorganic Chemistry, 45, 7581-7583 (2006).

(10) "Single-turnover intermolecular reaction between a FeIII-superoxide-CuI cytochrome c oxidase model and exogeneous Tyr244 mimics," J.P. Collman, R.A. Decreau, C. Sunderland, J. Chem. Comm., 3894-3896 (2006).

(11) "Mixed Azide-Terminated Monolayers: A Platform for Modifying Surfaces," J.P. Collman, N.K. Devaraj, T.A. Eberspacher, C.E.D. Chidsey, Langmuir, 22, 2457-2464 (2006).

(12) "Chemoselective Covalent Coupling of Oligonucleotide Probes to Self-Assembled Monolayers," Boyko, J.P. Collman, E.T. Kool, C.E.D. Chidsey, J. Am. Chem. Soc., 127, 8600-8601 (2005).