MichaelBarber

Michael Barber, D.Phil.

Assoc Dean, College Of Medicine Molecular Medicine

Assoc Dean & Dist Professor, College Of Medicine Molecular Medicine

Distinguished Professor, Cop Dept Of Pharmaceutical Science

Director, Graduate Certificate in Molecular Medicine, University of South Florida, College of Medicine

Director, Graduate Certificate in Health Sciences, University of South Florida, College of Medicine

Director, Graduate Certificate in Medical Biochemistry, Microbiology & Immunology, University of South Florida, College of Medicine

Director, Masters Program in Bioinformatics & Computational Biology, University of South Florida, College of Medicine

Director, Graduate Certificate in Biotechnology, University of South Florida, College of Medicine

Associate Dean for Graduate and Postdoctoral Affairs, College of Medicine - School of Biomedical Sciences, University of South Florida

Director, Graduate Certificate in Bioinformatics, University of South Florida, College of Medicine

Director, Graduate Certificate in Biochemistry & Molecular Biology, University of South Florida, College of Medicine

Director, Masters Program in Biochemistry & Molecular Biology, University of South Florida, College of Medicine

Contact Info 12901 Bruce B. Downs Blvd.
MDC 40
Tampa, FL 33612

Academic Email: mbarber@health.usf.edu

Academic Phone: (813) 974-9908

View My C.V.

Education

  • PHD, Biochemistry, University Of Sussex, 1976
  • M.Sc., Enzyme Chemistry, University of Kent, U.K., 1973
  • B.Sc. Hons., Chemistry, University of Kent, U.K., 1972

Interdisciplinary and Emerging Signature Programs

  • Cardiovascular

Research Interests

  • My research focuses on how enzymes containing novel metal atoms or other non-protein components enhance biological activity.

Memberships

  • Peer Review Committee 5C, Am. Heart Assoc., Florida/Puerto Rico Affiliate (Member, 2004 - 2007)
  • American Heart Assoc. Florida/Puerto Rico Affl. Hillsborough Community (Member, 2005 - 2006)

Recent Publications

  • Percy, MJ.Crowley, LJ.Roper, D.Vulliamy, TJ.Layton, DM.Barber, MJ. Identification and characterization of the novel FAD-binding lobe G75S mutation in cytochrome b(5) reductase: an aid to determine recessive congenital methemoglobinemia status in an infant. Blood cells, molecules & diseases. 36(1) : 81-90http://www.ncbi.nlm.nih.gov/pubmed/16310381
  • Percy, MJ.Crowley, LJ.Boudreaux, J.Barber, MJ. Expression of a novel P275L variant of NADH:cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding. Archives of biochemistry and biophysics. 447(1) : 59-67, 2006. http://www.ncbi.nlm.nih.gov/pubmed/16469290
  • Roma, GW.Crowley, LJ.Barber, MJ. Expression and characterization of a functional canine variant of cytochrome b5 reductase. Archives of biochemistry and biophysics. 452(1) : 69-82, 2006. http://www.ncbi.nlm.nih.gov/pubmed/16814740
  • Barber, MJ.Sampson, SN.Schneider, RK.Baszler, T.Tucker, RL. Use of magnetic resonance imaging to diagnose distal sesamoid bone injury in a horse. Journal of the American Veterinary Medical Association. 229(5) : 717-20, 2006. http://www.ncbi.nlm.nih.gov/pubmed/16948584
  • Percy, MJ.Crowley, LJ.Davis, CA.McMullin, MF.Savage, G.Hughes, J.McMahon, C.Quinn, RJ.Smith, O.Barber, MJ.Lappin, TR. Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase. British journal of haematology. 129(6) : 847-53, 2005. http://www.ncbi.nlm.nih.gov/pubmed/15953014
  • Roma, GW.Crowley, LJ.Davis, CA.Barber, MJ. Mutagenesis of Glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase. Biochemistry. 44(41) : 13467-76, 2005. http://www.ncbi.nlm.nih.gov/pubmed/16216070
  • Marohnic, CC.Crowley, LJ.Davis, CA.Smith, ET.Barber, MJ. Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis. Biochemistry. 44(7) : 2449-61, 2005. http://www.ncbi.nlm.nih.gov/pubmed/15709757
  • Davis, CA.Crowley, LJ.Barber, MJ. Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*. Archives of biochemistry and biophysics. 431(2) : 233-44, 2004. http://www.ncbi.nlm.nih.gov/pubmed/15488472
  • Davis, CA.Barber, MJ. Cytochrome b5 oxidoreductase: expression and characterization of the original familial ideopathic methemoglobinemia mutations E255- and G291D. Archives of biochemistry and biophysics. 425(2) : 123-32, 2004. http://www.ncbi.nlm.nih.gov/pubmed/15111120
  • Smith, ET.Davis, CA.Barber, MJ. Voltammetric simulations of multiple electron transfer/proton transfer coupled reactions: flavin adenine dinucleotide as a model system. Analytical biochemistry. 323(1) : 114-21, 2003. http://www.ncbi.nlm.nih.gov/pubmed/14622965
  • Bewley, MC.Davis, CA.Marohnic, CC.Taormina, D.Barber, MJ. The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site. Biochemistry. 42(45) : 13145-51, 2003. http://www.ncbi.nlm.nih.gov/pubmed/14609324
  • Marohnic, CC.Bewley, MC.Barber, MJ. Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase. Biochemistry. 42(38) : 11170-82, 2003. http://www.ncbi.nlm.nih.gov/pubmed/14503867
  • Davis, CA.Barber, MJ. Heterologous expression of enzymopenic methemoglobinemia variants using a novel NADH:cytochrome c reductase fusion protein. Protein expression and purification. 30(1) : 43-54, 2003. http://www.ncbi.nlm.nih.gov/pubmed/12821320
  • Pollock, VV.Conover, RC.Johnson, MK.Barber, MJ. Biotin sulfoxide reductase: Tryptophan 90 is required for efficient substrate utilization. Archives of biochemistry and biophysics. 409(2) : 315-26, 2003. http://www.ncbi.nlm.nih.gov/pubmed/12504898
  • Pollock, VV.Conover, RC.Johnson, MK.Barber, MJ. Bacterial expression of the molybdenum domain of assimilatory nitrate reductase: production of both the functional molybdenum-containing domain and the nonfunctional tungsten analog. Archives of biochemistry and biophysics. 403(2) : 237-48, 2002. http://www.ncbi.nlm.nih.gov/pubmed/12139973
  • Barber, MJ.Desai, SK.Marohnic, CC.Hernandez, HH.Pollock, VV. Synthesis and bacterial expression of a gene encoding the heme domain of assimilatory nitrate reductase. Archives of biochemistry and biophysics. 402(1) : 38-50, 2002. http://www.ncbi.nlm.nih.gov/pubmed/12051681
  • Davis, CA.Dhawan, IK.Johnson, MK.Barber, MJ. Heterologous expression of an endogenous rat cytochrome b(5)/cytochrome b(5) reductase fusion protein: identification of histidines 62 and 85 as the heme axial ligands. Archives of biochemistry and biophysics. 400(1) : 63-75, 2002. http://www.ncbi.nlm.nih.gov/pubmed/11913972
  • Cheltsov, AV.Barber, MJ.Ferreira, GC. Circular permutation of 5-aminolevulinate synthase. Mapping the polypeptide chain to its function. The Journal of biological chemistry. 276(22) : 19141-9, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11279050
  • Franco, R.Pereira, AS.Tavares, P.Mangravita, A.Barber, MJ.Moura, I.Ferreira, GC. Substitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin substrate-bound variants. The Biochemical journal. 356(Pt 1) : 217-22, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11336654
  • Marohnic, CC.Barber, MJ. Arginine 91 is not essential for flavin incorporation in hepatic cytochrome b(5) reductase. Archives of biochemistry and biophysics. 389(2) : 223-33, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11339812
  • Barber, MJ.Desai, SK.Marohnic, CC. Assimilatory nitrate reductase: lysine 741 participates in pyridine nucleotide binding via charge complementarity. Archives of biochemistry and biophysics. 394(1) : 99-110, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11566032
  • Barber, MJ.Quinn, GB. Production of a recombinant hybrid hemoflavoprotein: engineering a functional NADH:cytochrome c reductase. Protein expression and purification. 23(2) : 348-58, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11676611
  • Bewley, MC.Marohnic, CC.Barber, MJ. The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. Biochemistry. 40(45) : 13574-82, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11695905
  • Pollock, VV.Barber, MJ. Kinetic and mechanistic properties of biotin sulfoxide reductase. Biochemistry. 40(5) : 1430-40, 2001. http://www.ncbi.nlm.nih.gov/pubmed/11170471
  • Garton, SD.Temple, CA.Dhawan, IK.Barber, MJ.Rajagopalan, KV.Johnson, MK. Resonance Raman characterization of biotin sulfoxide reductase. Comparing oxomolybdenum enzymes in the ME(2)SO reductase family. The Journal of biological chemistry. 275(10) : 6798-805, 2000. http://www.ncbi.nlm.nih.gov/pubmed/10702237
  • Pollock, VV.Barber, MJ. Serine 121 is an essential amino acid for biotin sulfoxide reductase functionality. The Journal of biological chemistry. 275(45) : 35086-90, 2000. http://www.ncbi.nlm.nih.gov/pubmed/10948204
  • Kim, TH.Zhao, Y.Barber, MJ.Kuharsky, DK.Yin, XM. Bid-induced cytochrome c release is mediated by a pathway independent of mitochondrial permeability transition pore and Bax. The Journal of biological chemistry. 275(50) : 39474-81, 2000. http://www.ncbi.nlm.nih.gov/pubmed/10982793
  • Kluck, RM.Esposti, MD.Perkins, G.Renken, C.Kuwana, T.Bossy-Wetzel, E.Goldberg, M.Allen, T.Barber, MJ.Green, DR.Newmeyer, DD. The pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol. The Journal of cell biology. 147(4) : 809-22, 1999. http://www.ncbi.nlm.nih.gov/pubmed/10562282
  • Tan, D.Barber, MJ.Ferreira, GC. The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase. Protein science : a publication of the Protein Society. 7(5) : 1208-13, 1998. http://www.ncbi.nlm.nih.gov/pubmed/9605326
  • Barber, MJ.Trimboli, AJ.Nomikos, S.Smith, ET. Direct electrochemistry of the flavin domain of assimilatory nitrate reductase: effects of NAD+ and NAD+ analogs. Archives of biochemistry and biophysics. 345(1) : 88-96, 1997. http://www.ncbi.nlm.nih.gov/pubmed/9281315
  • Pollock, VV.Barber, MJ. Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme. The Journal of biological chemistry. 272(6) : 3355-62, 1997. http://www.ncbi.nlm.nih.gov/pubmed/9013576
  • Quinn, GB.Trimboli, AJ.Prosser, IM.Barber, MJ. Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH: nitrate reductase. Archives of biochemistry and biophysics. 327(1) : 151-60, 1996. http://www.ncbi.nlm.nih.gov/pubmed/8615685
  • Trimboli, AJ.Quinn, GB.Smith, ET.Barber, MJ. Thiol modification and site directed mutagenesis of the flavin domain of spinach NADH:nitrate reductase. Archives of biochemistry and biophysics. 331(1) : 117-26, 1996. http://www.ncbi.nlm.nih.gov/pubmed/8660690
  • Barber, MJ.Quinn, GB. High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase. Protein expression and purification. 8(1) : 41-7, 1996. http://www.ncbi.nlm.nih.gov/pubmed/8812833
  • Gong, J.Kay, CJ.Barber, MJ.Ferreira, GC. Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis. Biochemistry. 35(45) : 14109-17, 1996. http://www.ncbi.nlm.nih.gov/pubmed/8916896
  • Barber, MJ.Kay, CJ. Superoxide production during reduction of molecular oxygen by assimilatory nitrate reductase. Archives of biochemistry and biophysics. 326(2) : 227-32, 1996. http://www.ncbi.nlm.nih.gov/pubmed/8611027
  • Barber, MJ.Van Valkenburgh, H.Trimboli, AJ.Pollock, VV.Neame, PJ.Bastian, NR. The amino acid sequence of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Archives of biochemistry and biophysics. 320(2) : 266-75, 1995. http://www.ncbi.nlm.nih.gov/pubmed/7625833
  • Byvoet, P.Balis, JU.Shelley, SA.Montgomery, MR.Barber, MJ. Detection of hydroxyl radicals upon interaction of ozone with aqueous media or extracellular surfactant: the role of trace iron. Archives of biochemistry and biophysics. 319(2) : 464-9, 1995. http://www.ncbi.nlm.nih.gov/pubmed/7786029
  • Ferreira, GC.Vajapey, U.Hafez, O.Hunter, GA.Barber, MJ. Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis. Protein science : a publication of the Protein Society. 4(5) : 1001-6, 1995. http://www.ncbi.nlm.nih.gov/pubmed/7663334
  • Pollock, VV.Barber, MJ. Molecular cloning and expression of biotin sulfoxide reductase from Rhodobacter sphaeroides forma sp. denitrificans. Archives of biochemistry and biophysics. 318(2) : 322-32, 1995. http://www.ncbi.nlm.nih.gov/pubmed/7733660
  • Trimboli, AJ.Barber, MJ. Assimilatory nitrate reductase: reduction and inhibition by NADH/NAD+ analogs. Archives of biochemistry and biophysics. 315(1) : 48-53, 1994. http://www.ncbi.nlm.nih.gov/pubmed/7979404
  • Quinn, GB.Trimboli, AJ.Barber, MJ. Construction and expression of a flavocytochrome b5 chimera. The Journal of biological chemistry. 269(18) : 13375-81, 1994. http://www.ncbi.nlm.nih.gov/pubmed/8175767
  • Barber, MJ.Trimboli, AJ.McIntire, WS. The amino acid sequence of Pseudomonas putida azurin. Archives of biochemistry and biophysics. 303(1) : 22-6, 1993. http://www.ncbi.nlm.nih.gov/pubmed/8489263
  • Barber, MJ.Trimboli, AJ.Clark, M.Young, C.Neame, PJ. Purification and properties of Alligator mississipiensis cytochrome c. Archives of biochemistry and biophysics. 301(2) : 294-8, 1993. http://www.ncbi.nlm.nih.gov/pubmed/8384830
  • Cannons, AC.Barber, MJ.Solomonson, LP. Expression and characterization of the heme-binding domain of Chlorella nitrate reductase. The Journal of biological chemistry. 268(5) : 3268-71, 1993. http://www.ncbi.nlm.nih.gov/pubmed/8429004
  • Barber, MJ.Neame, PJ.Lim, LW.White, S.Matthews, FS. Correlation of x-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase. The Journal of biological chemistry. 267(10) : 6611-9, 1992. http://www.ncbi.nlm.nih.gov/pubmed/1551870
  • Kay, CJ.Solomonson, LP.Barber, MJ. Electrochemical and kinetic analysis of electron-transfer reactions of Chlorella nitrate reductase. Biochemistry. 30(48) : 11445-50, 1991. http://www.ncbi.nlm.nih.gov/pubmed/1742283
  • Bastian, NR.Kay, CJ.Barber, MJ.Rajagopalan, KV. Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans. The Journal of biological chemistry. 266(1) : 45-51, 1991. http://www.ncbi.nlm.nih.gov/pubmed/1845974
  • Barber, MJ.Neame, PJ. A conserved cysteine in molybdenum oxotransferases. The Journal of biological chemistry. 265(34) : 20912-5, 1990. http://www.ncbi.nlm.nih.gov/pubmed/2249998
  • Kay, CJ.Solomonson, LP.Barber, MJ. Oxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH. Biochemistry. 29(48) : 10823-8, 1990. http://www.ncbi.nlm.nih.gov/pubmed/2176886
  • Kay, CJ.Barber, MJ.Solomonson, LP.Kau, D.Cannons, AC.Hipkin, CR. Spectroscopic, thermodynamic and kinetic properties of Candida nitratophila nitrate reductase. The Biochemical journal. 272(2) : 545-8, 1990. http://www.ncbi.nlm.nih.gov/pubmed/2268283
  • Barber, MJ.Notton, BA. Spinach Nitrate Reductase : Effects of Ionic Strength and pH on the Full and Partial Enzyme Activities. Plant physiology. 93(2) : 537-540, 1990. http://www.ncbi.nlm.nih.gov/pubmed/16667499
  • Kay, CJ.Barber, MJ. Measurement of oxidation-reduction midpoint potentials by room temperature electron paramagnetic resonance potentiometry. Analytical biochemistry. 184(1) : 11-5, 1990. http://www.ncbi.nlm.nih.gov/pubmed/2157348
  • Kay, CJ.Barber, MJ.Notton, BA.Solomonson, LP. Oxidation--reduction midpoint potentials of the flavin, haem and Mo-pterin centres in spinach (Spinacia oleracea L.) nitrate reductase. The Biochemical journal. 263(1) : 285-7, 1989. http://www.ncbi.nlm.nih.gov/pubmed/2604699
  • Neame, PJ.Barber, MJ. Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase. The Journal of biological chemistry. 264(35) : 20894-901, 1989. http://www.ncbi.nlm.nih.gov/pubmed/2687265
  • Kay, CJ.Barber, MJ. EPR and kinetic analysis of the interaction of halides and phosphate with nitrate reductase. Biochemistry. 28(14) : 5750-8, 1989. http://www.ncbi.nlm.nih.gov/pubmed/2550063
  • Barber, MJ.Notton, BA.Kay, CJ.Solomonson, LP. Chloride Inhibition of Spinach Nitrate Reductase. Plant physiology. 90(1) : 70-74, 1989. http://www.ncbi.nlm.nih.gov/pubmed/16666771
  • Barber, MJ.Pollock, V.Spence, JT. Microcoulometric analysis of trimethylamine dehydrogenase. The Biochemical journal. 256(2) : 657-9, 1988. http://www.ncbi.nlm.nih.gov/pubmed/3223938
  • Kay, CJ.Barber, MJ.Solomonson, LP. Circular dichroism and potentiometry of FAD, heme and Mo-pterin prosthetic groups of assimilatory nitrate reductase. Biochemistry. 27(16) : 6142-9, 1988. http://www.ncbi.nlm.nih.gov/pubmed/2847786
  • Rosen, GM.Britigan, BE.Cohen, MS.Ellington, SP.Barber, MJ. Detection of phagocyte-derived free radicals with spin trapping techniques: effect of temperature and cellular metabolism. Biochimica et biophysica acta. 969(3) : 236-41, 1988. http://www.ncbi.nlm.nih.gov/pubmed/2835986
  • Spence, JT.Barber, MJ.Solomonson, LP. Stoichiometry of electron uptake and oxidation-reduction midpoint potentials of NADH:nitrate reductase. The Biochemical journal. 250(3) : 921-3, 1988. http://www.ncbi.nlm.nih.gov/pubmed/3390146
  • Terlesky, KC.Barber, MJ.Aceti, DJ.Ferry, JG. EPR properties of the Ni-Fe-C center in an enzyme complex with carbon monoxide dehydrogenase activity from acetate-grown Methanosarcina thermophila. Evidence that acetyl-CoA is a physiological substrate. The Journal of biological chemistry. 262(32) : 15392-5, 1987. http://www.ncbi.nlm.nih.gov/pubmed/2824458
  • Gardlik, S.Barber, MJ.Rajagopalan, KV. A molybdopterin-free form of xanthine oxidase. Archives of biochemistry and biophysics. 259(2) : 363-71, 1987. http://www.ncbi.nlm.nih.gov/pubmed/2827575
  • Eichler, DC.Solomonson, LP.Barber, MJ.McCreery, MJ.Ness, GC. Radiation inactivation analysis of enzymes. Effect of free radical scavengers on apparent target sizes. The Journal of biological chemistry. 262(20) : 9433-6, 1987. http://www.ncbi.nlm.nih.gov/pubmed/3298256
  • Barber, MJ.Eichler, DC.Solomonson, LP.Ackrell, BA. Anti-flavin antibodies. The Biochemical journal. 242(1) : 89-95, 1987. http://www.ncbi.nlm.nih.gov/pubmed/3109386
  • Barber, MJ.Notton, BA.Solomonson, LP. Oxidation-reduction midpoint potentials of the molybdenum center in spinach NADH:nitrate reductase. FEBS letters. 213(2) : 372-4, 1987. http://www.ncbi.nlm.nih.gov/pubmed/3030817
  • Solomonson, LP.McCreery, MJ.Kay, CJ.Barber, MJ. Radiation inactivation analysis of assimilatory NADH:nitrate reductase. Apparent functional sizes of partial activities associated with intact and proteolytically modified enzyme. The Journal of biological chemistry. 262(18) : 8934-9, 1987. http://www.ncbi.nlm.nih.gov/pubmed/3597400
  • Barber, MJ.Solomonson, LP.McCreery, MJ. Radiation inactivation of hepatic sulfite oxidase. Archives of biochemistry and biophysics. 256(1) : 260-4, 1987. http://www.ncbi.nlm.nih.gov/pubmed/3300554
  • Barber, MJ.Trudeau, W.Byvoet, P. Use of double spin-labeled histones to monitor histone-chromatin integration. Biochemical and biophysical research communications. 141(2) : 434-9, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3026383
  • Kay, CJ.Solomonson, LP.Barber, MJ. Thermodynamic properties of the heme prosthetic group in assimilatory nitrate reductase. The Journal of biological chemistry. 261(13) : 5799-802, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3700373
  • Solomonson, LP.Barber, MJ.Robbins, AP.Oaks, A. Functional domains of assimilatory NADH:nitrate reductase from Chlorella. The Journal of biological chemistry. 261(24) : 11290-4, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3015963
  • Capeillère-Blandin, C.Barber, MJ.Bray, RC. Comparison of the processes involved in reduction by the substrate for two homologous flavocytochromes b2 from different species of yeast. The Biochemical journal. 238(3) : 745-56, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3026360
  • Kay, CJ.Barber, MJ. Assimilatory nitrate reductase from Chlorella. Effect of ionic strength and pH on catalytic activity. The Journal of biological chemistry. 261(30) : 14125-9, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3771527
  • Barber, MJ.Solomonson, LP. The role of the essential sulfhydryl group in assimilatory NADH: nitrate reductase of Chlorella. The Journal of biological chemistry. 261(10) : 4562-7, 1986. http://www.ncbi.nlm.nih.gov/pubmed/3007465
  • Barber, MJ.Solomonson, LP.Eichler, DC. Spin-labeled erythrocyte membranes: direct identification of nitroxide-conjugated proteins. Biochemical and biophysical research communications. 127(3) : 793-8, 1985. http://www.ncbi.nlm.nih.gov/pubmed/2985057
  • Eichler, DC.Barber, MJ.Solomonson, LP. Anti-nitroxide immunoglobulin G: analysis of antibody specificity and their application as probes for spin-labeled proteins. Biochemistry. 24(5) : 1181-6, 1985. http://www.ncbi.nlm.nih.gov/pubmed/3006745
  • Solomonson, LP.Barber, MJ. Spin-labeled ouabain as a probe for cardiac glycoside receptor/Na, K-ATPase. Biochemical and biophysical research communications. 124(1) : 210-6, 1984. http://www.ncbi.nlm.nih.gov/pubmed/6093786
  • Solomonson, LP.Barber, MJ.Howard, WD.Johnson, JL.Rajagopalan, KV. Electron paramagnetic resonance studies on the molybdenum center of assimilatory NADH:nitrate reductase from Chlorella vulgaris. The Journal of biological chemistry. 259(2) : 849-53, 1984. http://www.ncbi.nlm.nih.gov/pubmed/6319388
  • Coughlan, MP.Mehra, RK.Barber, MJ.Siegel, LM. Optical and electron paramagnetic resonance spectroscopic studies on purine hydroxylase II from Aspergillus nidulans. Archives of biochemistry and biophysics. 229(2) : 596-603, 1984. http://www.ncbi.nlm.nih.gov/pubmed/6322698
  • Barber, MJ.Zektzer, AS.Rosen, GM.Dëmos, HA.Rauckman, EJ. Electron paramagnetic resonance studies of membrane proteins in hepatic microsomes. Biochimica et biophysica acta. 776(1) : 159-68, 1984. http://www.ncbi.nlm.nih.gov/pubmed/6089883
  • Barber, MJ.Siegel, LM. Electron paramagnetic resonance and potentiometric studies of arsenite interaction with the molybdenum centers of xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: a specific stabilization of the molybdenum(V) oxidation state. Biochemistry. 22(3) : 618-24, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6301524
  • Rosen, GM.Barber, MJ.Rauckman, EJ. Disruption of erythrocyte membranal organization by superoxide. The Journal of biological chemistry. 258(4) : 2225-8, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6296137
  • Barber, MJ.Rosen, GM.Siegel, LM.Rauckman, EJ. Evidence for formation of superoxide and formate radicals in Methanobacterium formicicum. Journal of bacteriology. 153(3) : 1282-6, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6298181
  • Barber, MJ.Rosen, GM.Rauckman, EJ. Studies of the mobility of maleimide spin labels within the erythrocyte membrane. Biochimica et biophysica acta. 732(1) : 126-32, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6307360
  • Janick, PA.Rueger, DC.Krueger, RJ.Barber, MJ.Siegel, LM. Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite. Biochemistry. 22(2) : 396-408, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6297547
  • Barber, MJ.Siegel, LM.Schauer, NL.May, HD.Ferry, JG. Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers. The Journal of biological chemistry. 258(18) : 10839-45, 1983. http://www.ncbi.nlm.nih.gov/pubmed/6309816
  • Barber, MJ.Siegel, LM. Oxidation-reduction potentials of molybdenum, flavin, and iron-sulfur centers in milk xanthine oxidase: variation with pH. Biochemistry. 21(7) : 1638-47, 1982. http://www.ncbi.nlm.nih.gov/pubmed/6896281
  • Barber, MJ.Salerno, JC.Siegel, LM. Magnetic interactions in milk xanthine oxidase. Biochemistry. 21(7) : 1648-56, 1982. http://www.ncbi.nlm.nih.gov/pubmed/6282313
  • Spence, JT.Barber, MJ.Siegel, LM. Determination of the stoichiometry of electron uptake and the midpoint reduction potentials of milk xanthine oxidase at 25 degrees C by microcoulometry. Biochemistry. 21(7) : 1656-61, 1982. http://www.ncbi.nlm.nih.gov/pubmed/6282314
  • Barber, MJ.Coughlan, MP.Kanda, M.Rajagopalan, KV. Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase. Archives of biochemistry and biophysics. 201(2) : 468-75, 1980. http://www.ncbi.nlm.nih.gov/pubmed/6249208
  • Bray, RC.Barber, MJ.Lowe, DJ. Electron-paramagnetic-resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid. The Biochemical journal. 171(3) : 653-8, 1978. http://www.ncbi.nlm.nih.gov/pubmed/208512
  • Williams-Smith, DL.Bray, RC.Barber, MJ.Tsopanakis, AD.Vincent, SP. Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy. The Biochemical journal. 167(3) : 593-600, 1977. http://www.ncbi.nlm.nih.gov/pubmed/23760
  • Barber, MJ.Bray, RC.Cammack, R.Coughlan, MP. Oxidation--reduction potentials of turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behaviour in molybdenum-containing hydroxylases. The Biochemical journal. 163(2) : 279-89, 1977. http://www.ncbi.nlm.nih.gov/pubmed/869927
  • Cammack, R.Barber, MJ.Bray, RC. Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase. The Biochemical journal. 157(2) : 469-78, 1976. http://www.ncbi.nlm.nih.gov/pubmed/183752
  • Barber, MJ.Bray, RC.Lowe, DJ.Coughlan, MP. Studies by electron-paramagnetic-resonance spectroscopy and stopped-flow spectrophotometry on the mechanism of action of turkey liver xanthine dehydrogenase. The Biochemical journal. 153(2) : 297-307, 1976. http://www.ncbi.nlm.nih.gov/pubmed/179533
  • Lowe, DJ.Barber, MJ.Pawlik, RT.Bray, RC. A new non-functional form of milk xanthine oxidase containing stable quinquivalent molybdenum. The Biochemical journal. 155(1) : 81-5, 1976. http://www.ncbi.nlm.nih.gov/pubmed/180983
  • Bray, RC.Barber, MJ.Dalton, H.Lowe, DJ.Coughlan, MP. Iron-sulphur systems in some isolated multi-component oxidative enzymes. Biochemical Society transactions. 3(4) : 479-82, 1975. http://www.ncbi.nlm.nih.gov/pubmed/1237425
  • Bray, RC.Lowe, DJ.Barber, MJ. Distribution of reducing equivalents on xanthine oxidase molecules and the rates of the intramolecular electron-transfer reactions. The Biochemical journal. 141(1) : 309-11, 1974. http://www.ncbi.nlm.nih.gov/pubmed/4375974

Positions Held

  • President (Faculty Council-College of Medicine, University of South Florida 2005 - 2006)
  • Professor (Department of Biochemistry & Molecular Biology, College of Medicine, University of South Florida 1991 - 2006)
  • Chair (LCME College of Medicine Evaluation Committee I - Institutional Setting: Governance and Administration, University of South Florida 2005 - 2006)
  • Member (AIMS Council-College of Medicine, University of South Florida 2005 - 2005)
  • Founding Member (Institute for Biomolecular Science, University of South Florida 1986 - 2002)
  • Director (Interdisciplinary Ph.D. Program in Cellular & Molecular Biology, University of South Florida Institute for Biomolecular Science 1994 - 1996)
  • Associate Director (Institute for Biomolecular Science, University of South Florida 1994 - 1996)
  • Associate Professor (Department of Biochemistry & Molecular Biology, College of Medicine, University of South Florida 1987 - 1991)
  • Assistant Professor (Department of Biochemistry, College of Medicine, University of South Florida 1983 - 1987)
  • Senior Research Associate (Department of Biochemistry, Medical School, Duke University 1981 - 1983)
  • Research Associate (Department of Biochemistry, Medical School, Duke University 1977 - 1981)
  • Lecturer (Department of Physical Sciences, Open University 1976 - 1977)
  • Predoctoral Fellow (School of Molecular Sciences, University of Sussex 1973 - 1977)

Awards/Honors

  • Commencement Marshal (University of South Florida - 2008)
  • Distinguished University Health Professor (University of South Florida, College of Medicine - 2007)
  • Graduate Education Award (Department of Molecular Medicine, University of South Florida, College of Medicine - 2007)
  • Grasso Award (Association of Medical Science Graduate Students, University of South Florida, College of Medicine - 2007)
  • Commencement Marshal (University of South Florida - 2007)
  • USF Health Distinguished Professor nomination (University of South Florida - 2007)
  • Fellow (USF Health Leadership Institute, University of South Florida, College of Medicine (Charter Class Mem - 2007)
  • University Distinguished Professor nomination (University of South Florida - 2006)
  • Whos Who Among Executives and Professionals 2006)
  • Outstanding Achievement Award, Department of Molecular Medicine (University of South Florida, College of Medicine - 2006)
  • Commencement Marshal (University of South Florida - 2006)
  • Commencement Marshal (University of South Florida - 2005)
  • University Distinguished Professor nomination (University of South Florida - 2005)
  • Commencement Marshal (University of South Florida, College of Medcine - 2004)
  • Who's Who in Medical Sciences Education 2004)
  • Who's Who in Sciences Higher Education 2004)
  • Commencement Marshal (University of South Florida - 2003)
  • Service First Award (State of Florida - 2002)