Education Ph.D Texas A&M University 1993 B.S. University of Texas, San Antonio 1988 NATO Postdoctoral Fellow 蒫ole Normale Sup閞ieure, Paris 1993-1994 NSF Postdoctoral Fellow, California Institute of Technology, Postdoctoral Researcher 1994-1995 Experience Assistant Professor of Chemistry University of California, Irvine 1995-2001 Associate Professor of Chemistry University of California, Irvine 2001-2005 Professor of Chemistry University of California, Irvine 2005-2009 Professor and Chair, Department of Chemistry and Biochemistry Baylor University 2009-

Inorganic and Bioinorganic Chemistry

Nature is an amazing chemist that is constantly synthesizing and transforming the world around us. Much of this work is done by enzymes, amazing little catalysts made of protein, just like you and me. Unlike industrial catalysts, enzymes work in water at mild temperatures and pressures. In many cases, enzymes with very similar active sites perform very different functions-- for example, identical Fe-heme cofactors bind and transport oxygen in hemoglobin and myoglobin, reduce oxygen in the cytochromes P450s and cytochrome oxidase, or nitrogen oxides in the nitrite and nitric oxide reductases. The substrate specificities and reactivity of the heme in the various enzymes is controlled by the protein environment around it, and small changes can have large effects. Likewise, the flow of electrons to a redox-active heme is also largely controled by the protein matrix it is contained in. Nature has amazing control over these electron transfers; redox sites are typically oriented so as to "aim" the electron towards its acceptor site, and triggering the flow to a specific chemical event.

Like nature, we try to use a controlled flow of electrons to initiate redox catalysis in hybrid heme enzymes. By varying the structures and environments of the hemes, we hope to make unique catalysts for different reactivities. These tailor-made enzymes are intended to perform useful chemical transformations driven simply by electricity or light. For example, by affixing the oxygen-binding protein myoglobin to an electrode we can make it catalyze the multi-electron reduction of nitrite to ammonia, a reaction that is important in plant metabolism. Using a P450, we can reduce carbon tetrachloride to methane, and amazing eight electron reduction that detoxifies this potent halocarbon. Binding photo-active Ru complexes to the surface of a protein allows us to photo-initiate electron flow into the heme active-site, and to control the reactions that occur there on the time-scale of a laser-pulse.

We are also interested in the redox chemistry of melanin, the black pigment in hair and skin. Melanins are catecholic pigments formed in melanocytes by oxidative polymerization of tyrosine. Melanins have very interesting photochemical properties; they are redox-active and tight binders of metal ions. Our recent work shows that they both mediate and generate reduced oxygen species. We are exploring the unique chemistry of melanins as a means of targeting melanoma, a cancer of the cells that make melanin.

“The Intricate Puzzle of HNO Chemistry” Patrick J. Farmer, Fabio Doctorovich. J. Inorg. Biochem. 2013, 118, 107. online 11/26/2012

“A singular variable decomposition approach for kinetic analysis of reactions of HNO with myoglobin” Zapata, A.; Pervitsky, D.; Kumar, M.R.; Farmer, P.J. J. Inorg. Biochem. 2013, 118, 171-178. online 10/13/2012

“Synthesis and characterization of lithium nitroxyl” Switzer, C.H.; Miller, T.W.; Farmer, P.J.; Fukuto, J.M. J. Inorg. Biochem. 2013, 118, 128-133. online 10/6/2012

“Studies on synthetic and natural melanin and its affinity for Fe(III) ion” Costa, T. G.; Younger, R.; Poe, C.; Farmer, P.J.; Szpoganicz, B. Bioinorg. Chem. Appl. 2012, 712840, 9 pp

“Direct oxygen imaging in titania nanocrystals” Lu, W.; Bruner, B.; Casillas, G.-C.; Mejía-Rosales, S.: Farmer, P.J.; Jose-Yacaman, M. Nanotechnology, 2012, 23, published online 8/4/2012.

“Probing motional behavior of eumelanin and pheomelanin by solid-state NMR: new insights into the pigment properties” Thureau, P.; Ziarelli, F.; Thévand, A.; Martin, R.W.; Farmer, P.J.; Viel, S.; Mollica, G. Chem. Euro. J. 2012, , published online 7/12/2012.

“Kinetic Characterization of a Slow-Binding Inhibitor of Bla2: Thiomaltol” Schlesinger, S.R.; Bruner, B.; Farmer, P.; Kim, S.-K. J. Enz. Inhib. Med. Chem. 2012, published online 1/11/2012.

“Large scale synthesis of V-shaped rutile twinned nanorods” Lu, W.; Bruner, B.; Garcia, G.-C.; He, J.: Jose-Yacaman, M.; Farmer, P.J. CrystEngComm, 2012, 14, 3120-3124.

“Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase” Kumar, M.R.; Zapata, A.; Ramirez, A.J.; Bowen, S.K.; Francisco, W.A.; Farmer, P.J. PNAS USA, 2011, 108, 18926-31.

“The Coordination Chemistry of HNO: From Warren Roper to Hemoglobin” Farmer, P.J.; Kumar, M.R; Almaraz, E. Comm. Inorg. Chem. 2010, 31, 1–14.

“Reactions of HNO with Heme Proteins: New Routes to HNO−Heme Complexes and Insight into Physiological Effects." Murugaeson R. Kumar, Jon M. Fukuto, Katrina M. Miranda and Patrick J. Farmer Inorg. Chem., 2010, 49 (14), pp 6283–6292

“Disulfiram, metals, and melanoma.” Walker, M.B.; Edwards, K.; Farmer, P.J. J. Chem. Educ., 2009, 86, 1224-1226.

“Pattern of Expression and Substrate Specificity of Chloroplast Ferredoxins from Chlamydomonas reinhardtii.” Terauchi, A.M.; Lu, S.-F.; Zaffagnini, M.; Tappa, S.; Hirasawa, M.; Tripathy, J.N.; Knaff, D.B.; Farmer, P.J.; Lemaire, S.D.; Hase, T.; Merchant, S.S. J. Biol. Chem., 2009, 284, 25867-25878.

“Photo- and thermal-induced linkage isomerizations in a peroxydithiocarbamate-Ru complex.” Ng, S.; Walker, M.B.; Farmer, P.J. Inorg. Chim. Acta, 2009, 362, 4013-4016.

“The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: Interactions at ferrous heme and cysteine thiols.” Miller, T.W.; Cherney, M.M.; Lee, A.J.; Francoleon, N.E.; Farmer, P.J.; King, S.B.; Hobbs, A.J.; Miranda, K.M.; Burstyn, J.N.; Fukoto, J.M. J. Biol. Chem., 2009, 284, 21788-21796.

“Nitrosyl Hydride (HNO) as an O2 Analogue: Long-Lived HNO Adducts of Ferrous Globins.” Kumar, M.R.; Pervitsky, D.; Chen, L.; Poulous , T.; Kundu, S.; Hargrove, M.S.; Rivera, E.J.; Diaz, A.; Colon, J.L.; Farmer, P.J. Biochemistry, 2009, 48, 5018-5025.

“Melansomal damage in normal human melanocytes induced by UVB and metal uptake-A basis for the pro-oxidant state of melanoma.” Gidanian, S.; Mentelle, M.; Meyskens, F.L.; Farmer, P.J. Photochem. Photobiol., 2008, 84, 556-564.

“Unexpected C-H Activation of Ru(II)-Dithiomaltol Complexes upon Oxidation.” Backlund, M.; Ziller, J.; Farmer, P.J. Inorg. Chem., 2008, 47, 2864-2870.

“Photolysis of the HNO Adduct of Myoglobin: Transient Generation of the Aminoxyl Radical.”Pervitsky, D.; Immoos, C.; van der Veer, W.; Farmer, P.J. J. Am. Chem. Soc., 2007, 129, 9590-9591.

“New perspectives on melanoma pathogenesis and chemoprevention.” Meyskens, F.L.; Farmer, P.J.; Yang, S.; Anton-Culver, H. Recent Res. Cancer, 2007, 174, 191-195.