Dale E. Edmondson

ORCID: 0000-0002-1304-231X
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Research Areas
  • Amino Acid Enzymes and Metabolism
  • Metal-Catalyzed Oxygenation Mechanisms
  • Metabolism and Genetic Disorders
  • Photosynthetic Processes and Mechanisms
  • Electrochemical sensors and biosensors
  • Electron Spin Resonance Studies
  • Parkinson's Disease Mechanisms and Treatments
  • Molecular Sensors and Ion Detection
  • Biochemical Analysis and Sensing Techniques
  • Microbial metabolism and enzyme function
  • Enzyme Catalysis and Immobilization
  • Polyamine Metabolism and Applications
  • Alcoholism and Thiamine Deficiency
  • Porphyrin Metabolism and Disorders
  • Metalloenzymes and iron-sulfur proteins
  • Enzyme Structure and Function
  • Synthesis and Biological Evaluation
  • Metal complexes synthesis and properties
  • Neurotransmitter Receptor Influence on Behavior
  • Porphyrin and Phthalocyanine Chemistry
  • Biochemical Acid Research Studies
  • Biochemical and Molecular Research
  • Receptor Mechanisms and Signaling
  • Biotin and Related Studies
  • Electrochemical Analysis and Applications

Emory University
2011-2022

University of Pavia
2003-2011

European Institute of Oncology
2010

Clemson University
2009

Pharmaxis (Australia)
2008

University of Alberta
2008

Acadia University
2008

Cornell University
2008

Newron Pharmaceuticals (Italy)
2007

University of Bari Aldo Moro
2007

Structures of human monoamine oxidase B (MAO B) in complex with safinamide and two coumarin derivatives, all sharing a common benzyloxy substituent, were determined by X-ray crystallography. These compounds competitively inhibit MAO Ki values the 0.1-0.5 microM range that are 30-700-fold lower than those observed A. The inhibitors bind noncovalently to B, occupying both entrance substrate cavities showing similarly oriented substituent.

10.1021/jm070677y article EN Journal of Medicinal Chemistry 2007-10-04

The three-dimensional structure of recombinant human monoamine oxidase A (hMAO A) as its clorgyline-inhibited adduct is described. Although the chain-fold hMAO similar to that rat MAO and B B), unique in it crystallizes a monomer exhibits solution hydrodynamic behavior monomeric form rather than dimeric A. A's active site consists single hydrophobic cavity ≈550 Å 3 , which smaller determined from deprenyl-inhibited (≈700 ) but larger (≈450 ). An important component loop conformation residues...

10.1073/pnas.0505975102 article EN Proceedings of the National Academy of Sciences 2005-08-29

Monoamine oxidase B (MAO-B) is an outer mitochondrial membrane-bound enzyme that catalyzes the oxidative deamination of arylalkylamine neurotransmitters and has been a target for number clinically used drug inhibitors. The 1.7-Å structure reversible isatin–MAO-B complex determined; it forms basis interpretation enzyme's when bound to either or irreversible 1,4-Diphenyl-2-butene found be MAO-B inhibitor, which occupies both entrance substrate cavity space in enzyme. Comparison these two...

10.1073/pnas.1633804100 article EN Proceedings of the National Academy of Sciences 2003-08-11

Abstract The inactivation of xanthine oxidase by cyanide is accompanied the extraction sulfur from protein which eliminated as thiocyanate. When carried out under anaerobic conditions, partial reduction enzyme occurs, equivalent to approximately a 2-electron uptake per eq thiocyanate released. Cyanide-inactivated can be largely reactivated incubation with Na2S. Experiments 35S-labeled Na2S reveal that reactivation reincorporation into protein. Treatment such results in again and elimination

10.1016/s0021-9258(18)62575-x article EN cc-by Journal of Biological Chemistry 1970-12-01

Incubation of the apoB2 subunit Escherichia coli ribonucleotide reductase with Fe 2+ and O 2 produces native B2, which contains tyrosyl radical-dinuclear iron cluster cofactor required for nucleotide reduction. The chemical mechanism this reconstitution reaction was investigated by stopped-flow absorption spectroscopy rapid freeze-quench EPR (electron paramagnetic resonance) spectroscopy. Two novel intermediates have been detected in reaction. first exhibits a broad band centered at 565...

10.1126/science.1650033 article EN Science 1991-07-19

10.1016/s0021-9258(18)50574-3 article EN cc-by Journal of Biological Chemistry 1979-06-01

LSD1 and LSD2 histone demethylases are implicated in a number of physiological pathological processes, ranging from tumorigenesis to herpes virus infection. A comprehensive structural, biochemical, cellular study is presented here probe the potential these enzymes for epigenetic therapies. This approach employs tranylcypromine as chemical scaffold design novel demethylase inhibitors. drug clinically validated antidepressant known target monoamine oxidases B. These two flavoenzymes...

10.1021/ja101557k article EN Journal of the American Chemical Society 2010-04-23

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTKinetic and spectroscopic characterization of intermediates component interactions in reactions methane monooxygenase from Methylococcus capsulatus (Bath)Katherine E. Liu, Ann M. Valentine, Danli Wang, Boi Hanh Huynh, Dale Edmondson, Anthanasios Salifoglou, Stephen J. LippardCite this: Am. Chem. Soc. 1995, 117, 41, 10174–10185Publication Date (Print):October 1, 1995Publication History Published online1 May 2002Published inissue 1 October...

10.1021/ja00146a002 article EN Journal of the American Chemical Society 1995-10-01

The R2 subunit of Escherichia coli ribonucleotide reductase (RNR) contains a stable tyrosyl radical (•Y122) diferric cluster cofactor. Earlier studies on the cofactor assembly reaction detected paramagnetic intermediate, X, that was found to be kinetically competent oxidize Y122. Studies using rapid freeze-quench (RFQ) Mössbauer and EPR spectroscopies led proposal X is comprised two high spin ferric ions S = 1/2 ligand radical, mutually coupled give ground state (Ravi, N.; Bollinger, J. M.,...

10.1021/ja960399k article EN Journal of the American Chemical Society 1996-01-01

Several reversible inhibitors selective for human monoamine oxidase B (MAO B) that do not inhibit MAO A have been described in the literature. The following compounds: 8-(3-chlorostyryl)caffeine, 1,4-diphenyl-2-butene, and trans,trans-farnesol are shown to competitively human, horse, rat, mouse with K(i) values low micromolar range but without effect on either bovine or sheep A. In contrast, competitive inhibitor isatin binds all known similar affinities. Sequence alignments crystal...

10.1074/jbc.m500949200 article EN cc-by Journal of Biological Chemistry 2005-02-15

Disposable plasticware such as test tubes, pipette tips, and multiwell assay or culture plates are used routinely in most biological research laboratories. Manufacturing of plastics requires the inclusion numerous chemicals to enhance stability, durability, performance. Some lubricating (slip) agents, exemplified by oleamide, also occur endogenously humans biologically active, cationic biocides included prevent bacterial colonization plastic surface. We demonstrate that these manufacturing...

10.1126/science.1162395 article EN Science 2008-11-06

The heme domain (iNOS(heme)) of inducible nitric oxide synthase (NOS) was expressed in Escherichia coli and purified to homogeneity. Rapid freeze-quench (RFQ) EPR used monitor the reaction reduced iNOS(heme) with oxygen presence absence substrate. In these reactions, oxidation occurs at a rate approximately 15 s(-)(1) 4 degrees C. A transient species g = 2.0 signal is also observed under conditions. spectral properties are those an anisotropic organic radical S (1)/(2). Comparison spectra...

10.1021/bi992026c article EN Biochemistry 1999-11-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism of Assembly the Tyrosyl Radical-Diiron(III) Cofactor E. Coli Ribonucleotide Reductase: 1. Moessbauer Characterization Diferric Radical PrecursorNatarajan Ravi, J. Martin Bollinger Jr., Boi Hanh Huynh, JoAnne Stubbe, and Dale EdmondsonCite this: Am. Chem. Soc. 1994, 116, 18, 8007–8014Publication Date (Print):September 1, 1994Publication History Published online1 May 2002Published inissue 1 September...

10.1021/ja00097a007 article EN Journal of the American Chemical Society 1994-09-01

The benzothiazinone BTZ043 is a tuberculosis drug candidate with nanomolar whole-cell activity. targets the DprE1 catalytic component of essential enzyme decaprenylphosphoryl-β-D-ribofuranose-2'-epimerase, thus blocking biosynthesis arabinans, vital components mycobacterial cell walls. Crystal structures DprE1, in its native form and complex BTZ043, reveal formation semimercaptal adduct between an active-site cysteine, as well contacts to neighboring lysine residue. Kinetic studies confirm...

10.1126/scitranslmed.3004395 article EN Science Translational Medicine 2012-09-05

Monoamine oxidase B (MAO B) is an outer mitochondrial membrane enzyme that catalyzes the oxidation of arylalkylamine neurotransmitters. The crystal structures MAO in complex with four N-propargylaminoindan class covalent inhibitors (rasagiline, N-propargyl-1(S)-aminoindan, 6-hydroxy-N-propargyl-1(R)-aminoindan, and N-methyl-N-propargyl-1(R)-aminoindan) have been determined at a resolution better than 2.1 Å. Rasagiline, N-methyl-N-propargyl-1(R)-aminoindan adopt essentially same conformation...

10.1021/jm031087c article EN Journal of Medicinal Chemistry 2004-02-27

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10.1016/s0021-9258(19)45598-1 article EN cc-by Journal of Biological Chemistry 1972-03-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFlavoprotein chemistry. I. Circular dichroism studies of the flavine chromophore and relation between redox properties environment in oxidases dehydrogenasesGordon Tollin Dale E. EdmondsonCite this: Biochemistry 1971, 10, 1, 113–124Publication Date (Print):January 5, 1971Publication History Published online1 May 2002Published inissue 5 January 1971https://doi.org/10.1021/bi00777a018RIGHTS & PERMISSIONSArticle Views247Altmetric-Citations117LEARN...

10.1021/bi00777a018 article EN Biochemistry 1971-01-05

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFlavoprotein chemistry. II. Chemical and physical characterization of the Shethna flavoprotein apoprotein kinetics thermodynamics flavine analog binding to apoproteinGordon Tollin Dale E. EdmondsonCite this: Biochemistry 1971, 10, 1, 124–132Publication Date (Print):January 5, 1971Publication History Published online1 May 2002Published inissue 5 January...

10.1021/bi00777a019 article EN Biochemistry 1971-01-05
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