Photo of Pierre T. Moenne-Loccoz, Ph.D.

Pierre T. Moenne-Loccoz Ph.D.

  • (503) 346-3429
    • Professor of Chemical Physiology and Biochemistry School of Medicine

University of Oregon, Postdoctoral Research Associate, Department of Chemistry, 1990-92

University College London, Department of Biology, 1992-93

Oregon Graduate Institute, Department of Biochemistry and Molecular Biology, 1993-96

OHSU/OGI School of Science & Engineering, Research Scientist, 1996-1999; Research Assistant Professor, 1999-2000; Assistant Professor, 2000-2007

OHSU, Institute of Environmental Health, Associate Professor, 2007-2018

Research interests: Structure-function relationships within proteins. Metalloenzymes and hemoproteins. Spectroscopic studies of enzymatic active sites, cofactors, and metal clusters. Reaction intermediates within catalysis. Nitric oxide in bioinorganic chemistry.

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Areas of interest

  • My lab studies families of metalloenzymes that contribute to microbial virulence by detoxifying nitric oxide (NO) generated by the host immune response. NO’s role in the immune response stems from its reactivity toward other radical species and transition metals and the production of toxic species. Microbial flavohemoglobins and other iron enzymes detoxify NO to inert nitrate and nitrous oxide through unknown reaction mechanisms. Another area of interest is how pathogens, commensal microbiota and their host compete for iron, an essential nutrient to most microorganisms. We study heme uptake and trafficking in pathogenic bacteria. Our research expertise combines molecular and magnetic spectroscopies with rapid kinetics to define reaction pathways.


  • Ph.D., University Pierre & Marie Curie, Paris VI, Paris France 1989


  • "Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase" Journal of the American Chemical Society  2001
  • "Heme oxidation in a chimeric protein of the α-selective Neisseriae meningitidis heme oxygenase with the distal helix of the δ-selective Pseudomonas aeruginosa" Biochemistry October 25 2005
  • "Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents" Journal of Biological Chemistry March 14 1997
  • "Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase" Biochemistry April 16 1996
  • "Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrate" Journal of Neuroscience April 20 2011
  • "Vibrational analysis of mononitrosyl complexes in hemerythrin and flavodiiron proteins" Journal of the American Chemical Society April 18 2012
  • "A low-spin alkylperoxo-iron(III) complex with weak Fe-O and O-O bonds" Journal of the American Chemical Society November 8 2006
  • "Structural, NMR spectroscopic, and computational investigation of hemin loading in the hemophore hasap from pseudomonas aeruginosa" Journal of the American Chemical Society July 21 2010
  • "O2 activation by non-heme diiron proteins" Biochemistry October 20 1998
  • "Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis" Biochemistry August 28 2007
  • "Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function" Biochemistry February 6 2001
  • "Nitric oxide dioxygenation reaction in devS and the initial response to nitric oxide in mycobacterium tuberculosis" Biochemistry February 15 2011
  • "Heme/Cu/O2 reactivity" Journal of the American Chemical Society October 13 2004
  • "Characterizing millisecond intermediates in hemoproteins using rapid-freeze-quench resonance Raman spectroscopy" Methods in molecular biology (Clifton, N.J.)  2014
  • "The millisecond intermediate in the reaction of nitric oxide with oxymyoglobin is an iron(III)-nitrato complex, not a peroxynitrite" Journal of the American Chemical Society June 3 2009
  • "Path of electron transfer in photosystem 1" Biochemistry  1994
  • "Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)" Journal of the American Chemical Society March 30 2005
  • "Reactivity studies on FeIII-(O2 2-)-Cu II compounds" Inorganic Chemistry August 6 2007
  • "Dioxygen and nitric oxide reactivity of a reduced heme/non-heme diiron(II) complex [(5L)Fe(II)···Fe(II)-Cl]+. Using a tethered tetraarylporphyrin for the development of an active site reactivity model for bacterial nitric oxide reductase" Inorganica Chimica Acta  2000
  • "Nitric oxide in biological denitrification" Chemical Reviews April 2002
  • "Proximal ligand electron donation and reactivity of the cytochrome P450 ferric-peroxo anion" Journal of the American Chemical Society April 18 2012
  • "Coupled oxidation vs heme oxygenation" Journal of the American Chemical Society April 9 2003
  • "Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae" Protein Expression and Purification April 1 2003
  • "Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins" Journal of the American Chemical Society February 3 2010
  • "Purification and characterization of the MQH2" Journal of Biological Chemistry September 19 2003
  • "Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins" Natural Product Reports  2007
  • "Structural characterization of the catalytic high-spin heme b of nitric oxide reductase" Journal of the American Chemical Society June 3 1998
  • "Formation and characterization of a high-spin heme-copper dioxygen (peroxo) complex [8]" Journal of the American Chemical Society October 27 1999
  • "Accessibility of the distal heme face, rather than Fe-His bond strength, determines the heme-nitrosyl coordination number of cytochromes c′" Biochemistry June 21 2005
  • "Biochemistry" Science December 17 2010

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