Marc Fontecave

Articles in Scholarly Journals [Incomplete List]

  1. The SUF iron–sulfur cluster biosynthetic machinery: Sulfur transfer from the SUFS–SUFE complex to SUFA
    FEBS Letters, vol. 581, no. 7, pp. 1362–1368, 2007
  2. Ru- and Fe-based N,N'-bis(2-pyridylmethyl)-N-methyl-(1S,2S)-1,2-cyclohexanediamine complexes immobilised on mesoporous MCM-41: Synthesis, characterization and catalytic applications
    Journal of Molecular Catalysis A: Chemical, vol. 270, no. 1-2, pp. 132–143, 2007
  3. MiaB, a Bifunctional Radical-S-Adenosylmethionine Enzyme Involved in the Thiolation and Methylation of tRNA, Contains Two Essential [4Fe-4S] Clusters
    Biochemistry, vol. 46, no. 17, pp. 5140–5147, 2007
  4. Cobaloximes as Functional Models for Hydrogenases. 2. Proton Electroreduction Catalyzed by Difluoroborylbis(dimethylglyoximato)cobalt(II) Complexes in Organic Media
    Inorganic Chemistry, vol. 46, no. 5, pp. 1817–1824, 2007
  5. SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly
    Journal of Biological Chemistry, vol. 282, no. 18, pp. 13342–13350, 2007
  6. Iron-Sulfur Cluster Biosynthesis: CHARACTERIZATION OF ESCHERICHIA COLI CYaY AS AN IRON DONOR FOR THE ASSEMBLY OF [2Fe-2S] CLUSTERS IN THE SCAFFOLD IscU
    Journal of Biological Chemistry, vol. 281, no. 24, pp. 16256–16263, 2006
  7. Dinucleotide Spore Photoproduct, a Minimal Substrate of the DNA Repair Spore Photoproduct Lyase Enzyme from Bacillus subtilis
    Journal of Biological Chemistry, vol. 281, no. 37, pp. 26922–26931, 2006
  8. Iron-sulfur clusters: ever-expanding roles
    Nature Chemical Biology, vol. 2, no. 4, Article ID nchembio0406-171, 3 pages, 2006
  9. The spore photoproduct lyase repairs the 5S- and not the 5R-configured spore photoproduct DNA lesion
    Chemical Communications, no. 4, p. 445, 2006
  10. Sequence-Specific Nucleic Acid Damage Induced by Peptide Nucleic Acid Conjugates That Can Be Enzyme-Activated
    Angewandte Chemie International Edition, vol. 45, no. 41, pp. 6859–6861, 2006
  11. Activation of the Anaerobic Ribonucleotide Reductase byS-Adenosylmethionine
    ChemBioChem, vol. 6, no. 11, pp. 1960–1962, 2005
  12. DNA Detection through Signal Amplification by Using NADH:Flavin Oxidoreductase and Oligonucleotide-Flavin Conjugates as Cofactors
    Angewandte Chemie International Edition, vol. 44, no. 18, pp. 2764–2767, 2005
  13. Mechanisms of iron–sulfur cluster assembly: the SUF machinery
    JBIC Journal of Biological Inorganic Chemistry, vol. 10, no. 7, pp. 713–721, 2005
  14. Some general principles for designing electrocatalysts with hydrogenase activity
    Coordination Chemistry Reviews, vol. 249, no. 15-16, pp. 1518–1535, 2005
  15. The flavin reductase ActVB from Streptomyces coelicolor: Characterization of the electron transferase activity of the flavoprotein form
    FEBS Letters, vol. 579, no. 13, pp. 2817–2820, 2005
  16. Quinolinate synthetase, an iron–sulfur enzyme in NAD biosynthesis
    FEBS Letters, vol. 579, no. 17, pp. 3737–3743, 2005
  17. Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from
    FEBS Letters, vol. 579, no. 22, pp. 5055–5060, 2005
  18. The Journal of Organic Chemistry, vol. 70, no. 1, pp. 301–308, 2005
  19. Inorganic Chemistry, vol. 44, no. 13, pp. 4786–4795, 2005
  20. Analysis of the Heteromeric CsdA-CsdE Cysteine Desulfurase, Assisting Fe-S Cluster Biogenesis in Escherichia coli
    Journal of Biological Chemistry, vol. 280, no. 29, pp. 26760–26769, 2005
  21. An Aromatic Hydroxylation Reaction Catalyzed by a Two-component FMN-dependent Monooxygenase: THE ActVA-ActVB SYSTEM FROM STREPTOMYCES COELICOLOR
    Journal of Biological Chemistry, vol. 281, no. 1, pp. 27–35, 2005
  22. The [Fe-Fe]-Hydrogenase Maturation Protein HydF from Thermotoga maritima Is a GTPase with an Iron-Sulfur Cluster
    Journal of Biological Chemistry, vol. 281, no. 2, pp. 769–774, 2005
  23. A Two-component Flavin-dependent Monooxygenase Involved in Actinorhodin Biosynthesis in Streptomyces coelicolor
    Journal of Biological Chemistry, vol. 279, no. 43, pp. 44362–44369, 2004
  24. MiaB Protein Is a Bifunctional Radical-S-Adenosylmethionine Enzyme Involved in Thiolation and Methylation of tRNA
    Journal of Biological Chemistry, vol. 279, no. 46, pp. 47555–47563, 2004
  25. Biochemistry, vol. 43, no. 27, pp. 8815–8825, 2004
  26. New flavin and deazaflavin oligonucleotide conjugates for the amperometric detection of DNA hybridization
    Chemical Communications, no. 14, p. 1624, 2004
  27. S-adenosylmethionine: nothing goes to waste
    Trends in Biochemical Sciences, vol. 29, no. 5, pp. 243–249, 2004
  28. SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly
    JBIC Journal of Biological Inorganic Chemistry, vol. 9, no. 7, pp. 828–838, 2004
  29. Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of SufA from Escherichia coli involved in Fe-S cluster biosynthesis
    Journal of Biomolecular NMR, vol. 30, no. 3, pp. 379–380, 2004
  30. Crystallization-Induced Asymmetric Transformation of Chiral-at-metal Ruthenium(II) Complexes Bearing Achiral Ligands
    Chemistry - A European Journal, vol. 10, no. 10, pp. 2548–2554, 2004
  31. Mechanistic Tuning of Hydrocarbon Oxidations with H2O2, Catalyzed by Hexacoordinate Ferrous Complexes
    European Journal of Inorganic Chemistry, vol. 2004, no. 15, pp. 3163–3171, 2004
  32. Mechanistic studies of the SufS–SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE
    FEBS Letters, vol. 555, no. 2, pp. 263–267, 2003
  33. Synthesis of 8-vinyladenosine 5'-di- and 5'-triphosphate: evaluation of the diphosphate compound on ribonucleotide reductase
    Tetrahedron, vol. 59, no. 37, pp. 7315–7322, 2003
  34. Bioinorganic Chemistry Special Feature: A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase
    Proceedings of the National Academy of Sciences, vol. 100, no. 7, pp. 3826–3831, 2003
  35. SufA from Erwinia chrysanthemi. CHARACTERIZATION OF A SCAFFOLD PROTEIN REQUIRED FOR IRON-SULFUR CLUSTER ASSEMBLY
    Journal of Biological Chemistry, vol. 278, no. 20, pp. 17993–18001, 2003
  36. MiaB Protein from Thermotoga maritima: CHARACTERIZATION OF AN EXTREMELY THERMOPHILIC tRNA-METHYLTHIOTRANSFERASE
    Journal of Biological Chemistry, vol. 278, no. 32, pp. 29515–29524, 2003
  37. Biogenesis of Fe-S Cluster by the Bacterial Suf System: SufS AND SufE FORM A NEW TYPE OF CYSTEINE DESULFURASE
    Journal of Biological Chemistry, vol. 278, no. 40, pp. 38352–38359, 2003
  38. Journal of the American Chemical Society, vol. 125, no. 1, pp. 38–39, 2003
  39. Inorganic Chemistry, vol. 42, no. 2, pp. 499–507, 2003
  40. Inorganic Chemistry, vol. 42, no. 16, pp. 4810–4816, 2003
  41. Inorganic Chemistry, vol. 42, no. 24, pp. 8110–8116, 2003
  42. Chemical Reviews, vol. 103, no. 6, pp. 2149–2166, 2003
  43. Biochemistry, vol. 41, no. 29, pp. 9145–9152, 2002
  44. Biochemistry, vol. 41, no. 32, pp. 10360–10368, 2002
  45. Reductive Cleavage of S-Adenosylmethionine by Biotin Synthase from Escherichia coli
    Journal of Biological Chemistry, vol. 277, no. 16, pp. 13449–13454, 2002
  46. Mechanism and Substrate Specificity of the Flavin Reductase ActVB from Streptomyces coelicolor
    Journal of Biological Chemistry, vol. 278, no. 1, pp. 296–303, 2002
  47. Enzymatic Modification of tRNAs. MiaB IS AN IRON-SULFUR PROTEIN
    Journal of Biological Chemistry, vol. 277, no. 16, pp. 13367–13370, 2002
  48. Identification of Iron(III) Peroxo Species in the Active Site of the Superoxide Reductase SOR from Desulfoarculus baarsii
    Journal of the American Chemical Society, vol. 124, no. 18, pp. 4966–4967, 2002
  49. BioMetals, vol. 15, no. 4, pp. 341–346, 2002
  50. The PLP-dependent biotin synthase from Escherichia coli: mechanistic studies
    FEBS Letters, vol. 532, no. 3, pp. 465–468, 2002
  51. Biochemical and electron paramagnetic resonance study of the iron superoxide dismutase from Plasmodium falciparum
    Molecular and Biochemical Parasitology, vol. 120, no. 2, pp. 237–246, 2002
  52. Fluorescent Deazaflavin-Oligonucleotide Probes for Selective Detection of DNA
    Angewandte Chemie International Edition, vol. 41, no. 3, pp. 486–489, 2002
  53. A Diferric Peroxo Complex with an Unprecedented Spin Configuration: AnS=2 System Arising from anS=5/2, 1/2 Pair
    Angewandte Chemie International Edition, vol. 41, no. 4, pp. 617–620, 2002
  54. Sulfide Oxidation by Hydrogen Peroxide Catalyzed by Iron Complexes: Two Metal Centers Are Better Than One
    Chemistry - A European Journal, vol. 8, no. 5, p. 1196, 2002
  55. H2O2-Dependent Fe-Catalyzed Oxidations: Control of the Active Species
    Angewandte Chemie International Edition, vol. 40, no. 5, pp. 949–952, 2001
  56. The iron-sulfur center of biotin synthase: site-directed mutants
    JBIC Journal of Biological Inorganic Chemistry, vol. 7, no. 1-2, pp. 83–93, 2001
  57. Adenosylmethionine as a source of 5'-deoxyadenosyl radicals
    Current Opinion in Chemical Biology, vol. 5, no. 5, pp. 506–512, 2001
  58. Pulse radiolysis studies on superoxide reductase from Treponema pallidum
    FEBS Letters, vol. 497, no. 2-3, pp. 171–173, 2001
  59. Re-examination of the formation of dinitrosyl–iron complexes during reaction of S-nitrosothiols with Fe(II)
    Inorganica Chimica Acta, vol. 318, no. 1-2, pp. 1–7, 2001
  60. Activation of Class III Ribonucleotide Reductase by Thioredoxin
    Journal of Biological Chemistry, vol. 276, no. 13, pp. 9587–9589, 2001
  61. Iron-Sulfur Cluster Assembly. CHARACTERIZATION OF IscA AND EVIDENCE FOR A SPECIFIC AND FUNCTIONAL COMPLEX WITH FERREDOXIN
    Journal of Biological Chemistry, vol. 276, no. 25, pp. 22604–22607, 2001
  62. Activation of cyclohexylhydroperoxide by diiron complexes: a new route for selective peroxide decomposition
    Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry, vol. 4, no. 1, pp. 27–34, 2001
  63. Mechanisms of formation of free radicals in biological catalysis
    Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry, vol. 4, no. 7, pp. 531–538, 2001
  64. An easy electrochemical procedure for tailoring thin films containing the [Fe(bpy)2(CH3CN)2]2+ and/or [Fe(bpy)3]2+-like cores (bpy=2,2'-bipyridine). Application to the design of a modified electrode with a supramolecular structure
    Electrochemistry Communications, vol. 3, no. 12, pp. 686–691, 2001
  65. Biochemistry, vol. 40, no. 12, pp. 3730–3736, 2001
  66. Biochemistry, vol. 40, no. 16, pp. 5032–5040, 2001
  67. Biochemistry, vol. 40, no. 23, pp. 6713–6719, 2001
  68. Journal of the American Chemical Society, vol. 123, no. 13, pp. 3048–3054, 2001
  69. Biochemistry, vol. 39, no. 14, pp. 4165–4173, 2000
  70. Hydroxylation of alkanes catalysed by a chiral µ-oxo diferric complex: a metal-based mechanism
    Journal of Molecular Catalysis A: Chemical, vol. 156, no. 1-2, pp. 85–89, 2000
  71. A Simplifed Functional Version of the Escherichia coli Sulfite Reductase
    Journal of Biological Chemistry, vol. 275, no. 48, pp. 37651–37656, 2000
  72. Reaction of the Desulfoferrodoxin from Desulfoarculus baarsii with Superoxide Anion. EVIDENCE FOR A SUPEROXIDE REDUCTASE ACTIVITY
    Journal of Biological Chemistry, vol. 275, no. 1, pp. 115–121, 2000
  73. The Activating Component of the Anaerobic Ribonucleotide Reductase from Escherichia coli. AN IRON-SULFUR CENTER WITH ONLY THREE CYSTEINES
    Journal of Biological Chemistry, vol. 275, no. 21, pp. 15669–15675, 2000
  74. Journal of Organic Chemistry, vol. 65, no. 1, pp. 249–253, 2000
  75. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module
    Journal of Molecular Biology, vol. 299, no. 1, pp. 199–212, 2000
  76. Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli
    Journal of Biological Inorganic Chemistry, vol. 4, no. 5, pp. 614–620, 1999
  77. Electrochemical behaviour of (µ-oxo) di-aqua diiron(III) complexes in organic media. Electrogeneration of mononuclear [FeII(L)2(S)2]2+ complexes (L=2,2'-bipyridine and (-)4,5-pinene-2,2'-bipyridine; S=H2O or CH3CN)
    Journal of Electroanalytical Chemistry, vol. 469, no. 1, pp. 53–62, 1999
  78. The lipoate synthase from Escherichia coli is an iron-sulfur protein
    FEBS Letters, vol. 453, no. 1-2, pp. 25–28, 1999
  79. Glycyl radical enzymes: a conservative structural basis for radicals
    Structure, vol. 7, no. 11, pp. R257–R262, 1999
  80. BioMetals, vol. 12, no. 3, pp. 195–199, 1999
  81. Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride
    Biochemical Journal, vol. 342, no. 2, p. 465, 1999
  82. 31P Nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase
    European Journal of Biochemistry, vol. 261, no. 2, pp. 430–437, 1999
  83. An active ribonucleotide reductase from Arabidopsis thaliana . Cloning, expression and characterization of the large subunit
    European Journal of Biochemistry, vol. 266, no. 1, pp. 62–69, 1999
  84. Calcein as a Fluorescent Probe for Ferric Iron. APPLICATION TO IRON NUTRITION IN PLANT CELLS
    Journal of Biological Chemistry, vol. 274, no. 19, pp. 13375–13383, 1999
  85. The NAD(P)H:Flavin Oxidoreductase from Escherichia coli. EVIDENCE FOR A NEW MODE OF BINDING FOR REDUCED PYRIDINE NUCLEOTIDES
    Journal of Biological Chemistry, vol. 274, no. 26, pp. 18252–18260, 1999
  86. The Anaerobic Ribonucleotide Reductase from Escherichia coli. THE SMALL PROTEIN IS AN ACTIVATING ENZYME CONTAINING A [4Fe-4S]2+ CENTER
    Journal of Biological Chemistry, vol. 274, no. 44, pp. 31291–31296, 1999
  87. Biochemistry, vol. 38, no. 22, pp. 7040–7049, 1999
  88. Inorganic Chemistry, vol. 38, no. 6, pp. 1261–1268, 1999
  89. Journal of the American Chemical Society, vol. 121, no. 27, pp. 6344–6350, 1999
  90. Journal of the American Chemical Society, vol. 120, no. 51, pp. 13370–13382, 1998
  91. Biochemistry, vol. 37, no. 17, pp. 6114–6123, 1998
  92. Biochemistry, vol. 37, no. 34, pp. 11879–11887, 1998
  93. Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana . Comparison with Escherichia coli and mouse
    European Journal of Biochemistry, vol. 258, no. 2, pp. 485–490, 1998
  94. Flavin-oligonucleotide conjugates: sequence specific photocleavage of DNA
    Chemical Communications, no. 22, pp. 2457–2458, 1998
  95. Resveratrol, a remarkable inhibitor of ribonucleotide reductase
    FEBS Letters, vol. 421, no. 3, pp. 277–279, 1998
  96. Oxidations by copper metalloenzymes and some biomimetic approaches
    Coordination Chemistry Reviews, vol. 170, no. 1, pp. 125–140, 1998
  97. Functional models of non-heme diiron enzymes
    Coordination Chemistry Reviews, vol. 178-180, pp. 1555–1572, 1998
  98. The Flavoprotein Component of theEscherichia coliSulfite Reductase Can Act as a Cytochrome P450c17 Reductase
    Biochemical and Biophysical Research Communications, vol. 246, no. 3, pp. 602–605, 1998
  99. A Reagentless Biosensor for the Amperometric Determination of NADH
    Electroanalysis, vol. 10, no. 8, pp. 521–525, 1998
  100. The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis
    Acta Crystallographica Section D Biological Crystallography, vol. 54, no. 1, pp. 135–136, 1998
  101. Mixed-valent μ-oxo-bridged diiron complexes produced by radiolytic reduction at 77 K studied by EPR
    Journal of Biological Inorganic Chemistry, vol. 2, no. 2, pp. 242–255, 1997
  102. The role of exogenous iron in the activation of ribonucleotide reductase from Escherichia coli
    Journal of Biological Inorganic Chemistry, vol. 2, no. 4, pp. 418–426, 1997
  103. Ribonucleotide reductase from the higher plant Arabidopsis thaliana : expression of the R2 component and characterization of its iron-radical center
    Journal of Biological Inorganic Chemistry, vol. 2, no. 5, pp. 586–594, 1997
  104. µ-Oxo diferric complexes as oxidation catalysts with hydrogen peroxide and their potential in asymmetric oxidation
    Tetrahedron Letters, vol. 38, no. 21, pp. 3727–3730, 1997
  105. Journal of Organic Chemistry, vol. 62, no. 11, pp. 3520–3528, 1997
  106. Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes?
    Proceedings of the National Academy of Sciences, vol. 94, no. 2, pp. 475–478, 1997
  107. Biochemistry, vol. 36, no. 19, pp. 5921–5928, 1997
  108. Inorganic Chemistry, vol. 36, no. 27, pp. 6148–6149, 1997
  109. Biochemistry, vol. 35, no. 26, pp. 8595–8602, 1996
  110. The Free Radical of the Anaerobic Ribonucleotide Reductase from Escherichia coli Is at Glycine 681
    Journal of Biological Chemistry, vol. 271, no. 12, pp. 6827–6831, 1996
  111. The Anaerobic Escherichia coli Ribonucleotide Reductase
    Journal of Biological Chemistry, vol. 271, no. 16, pp. 9410–9416, 1996
  112. Is the NAD(P)H:Flavin Oxidoreductase from Escherichia coli a Member of the Ferredoxin-NADP+ Reductase Family?. EVIDENCE FOR THE CATALYTIC ROLE OF SERINE 49RESIDUE
    Journal of Biological Chemistry, vol. 271, no. 28, pp. 16656–16661, 1996
  113. Alkane oxidation catalyzed by $mu;-oxo bridged diferric complexes: an overall mechanism
    Journal of Molecular Catalysis A: Chemical, vol. 113, no. 1-2, pp. 61–75, 1996
  114. The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals
    FEBS Letters, vol. 387, no. 2-3, pp. 137–140, 1996
  115. Dynamic equilibria in iron uptake and release by ferritin
    BioMetals, vol. 9, no. 3, pp. 303–309, 1996
  116. Aromatic Hydroxylation by H2O2 and O2 Catalyzed by aµ-Oxo Diiron(III) Complex
    Angewandte Chemie International Edition in English, vol. 35, no. 20, pp. 2353–2355, 1996
  117. Formation of an Alkylperoxoiron(III) Complex during Oxidations Catalyzed byµ-Oxodiiron(III) Complexes
    Angewandte Chemie International Edition in English, vol. 34, no. 2, pp. 203–205, 1995
  118. A New Type of Trinuclear Oxoiron(III) Cluster
    Angewandte Chemie International Edition in English, vol. 34, no. 2, pp. 205–207, 1995
  119. The Mechanism of the Anaerobic Escherichia coli Ribonucleotide Reductase Investigated with Nuclear Magnetic Resonance Spectroscopy
    Biochemical and Biophysical Research Communications, vol. 214, no. 1, pp. 28–35, 1995
  120. Selective 5â?²-desilylation of 3â?²,5â?²-disilyi AraU derivatives under basic conditions
    Tetrahedron Letters, vol. 36, no. 52, pp. 9479–9480, 1995
  121. NMR studies of binding of 5-FdUDP and dCDP to ribonucleoside-diphosphate reductase from Escherichia coli
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1247, no. 2, pp. 284–292, 1995
  122. NADPH-sulfite reductase flavoprotein from Escherichia coli: Contribution to the flavin content and subunit interaction
    FEBS Letters, vol. 374, no. 1, pp. 82–84, 1995
  123. Decomposition of FK 409, a new vasodilator: Identification of nitric oxide as a metabolite
    Bioorganic & Medicinal Chemistry Letters, vol. 5, no. 9, pp. 973–978, 1995
  124. Copper amine oxidase: a novel use for a tyrosine
    Structure, vol. 3, no. 11, pp. 1127–1129, 1995
  125. The Flavin Reductase Activity of the Flavoprotein Component of Sulfite Reductase from Escherichia coli
    Journal of Biological Chemistry, vol. 270, no. 35, pp. 20550–20555, 1995
  126. The Mechanism and Substrate Specificity of the NADPH:Flavin Oxidoreductase from Escherichia coli
    Journal of Biological Chemistry, vol. 270, no. 51, pp. 30392–30400, 1995
  127. Formate is the Hydrogen Donor for the Anaerobic Ribonucleotide Reductase from Escherichia coli
    Proceedings of the National Academy of Sciences, vol. 92, no. 19, pp. 8759–8762, 1995
  128. Biochemistry, vol. 34, no. 16, pp. 5411–5418, 1995
  129. Journal of the American Chemical Society, vol. 117, no. 43, pp. 10713–10719, 1995
  130. Journal of Organic Chemistry, vol. 59, no. 23, pp. 7019–7026, 1994
  131. Oxidation of alkanes catalyzed by binuclear metal complexes: Control by the coordination sphere
    Tetrahedron Letters, vol. 35, no. 34, pp. 6287–6290, 1994
  132. Ferric Reductases in Escherichia coli: The Contribution of the Hemoglobin-like Protein
    Biochemical and Biophysical Research Communications, vol. 198, no. 1, pp. 127–131, 1994
  133. Sulfite Reductase of Escherichia coli Is a Ferrisiderophore Reductase
    Biochemical and Biophysical Research Communications, vol. 192, no. 3, pp. 1403–1408, 1993
  134. 19F NMR Study of the Interaction of Fluoride Ion with Ribonucleotide Reductase and Methane Monooxygenase
    Biochemical and Biophysical Research Communications, vol. 195, no. 2, pp. 594–599, 1993
  135. Flavodoxin Is Required for the Activation of the Anaerobic Ribonucleotide Reductase
    Biochemical and Biophysical Research Communications, vol. 197, no. 2, pp. 792–797, 1993
  136. Iron: Metabolism, toxicity and therapy
    Biochimie, vol. 75, no. 9, pp. 767–773, 1993
  137. Inorganic Chemistry, vol. 32, no. 22, pp. 4766–4773, 1993
  138. Biochemistry, vol. 31, no. 3, pp. 780–786, 1992
  139. 8-azidoadenosine and ribonucleotide reductase
    Biochemical and Biophysical Research Communications, vol. 187, no. 1, pp. 432–437, 1992
  140. Multifield Saturation Magnetization Measurements of Oxidized and Reduced Ribonucleotide Reductase fromEscherichia coli
    Angewandte Chemie International Edition in English, vol. 31, no. 11, pp. 1513–1515, 1992
  141. Reduction of the Small Subunit of Ribonucleotide Reductase by Diimide: Evidence for the Formation of the Mixed-Valence FeII?FeIII center
    Angewandte Chemie International Edition in English, vol. 30, no. 9, pp. 1135–1136, 1991
  142. Oxygen-Sensitive Ribonucleoside Triphosphate Reductase is Present in Anaerobic Escherichia coli
    Proceedings of the National Academy of Sciences, vol. 86, no. 7, pp. 2147–2151, 1989
  143. Journal of the American Chemical Society, vol. 106, no. 18, pp. 5217–5222, 1984
  144. Oxidation of monosubstituted olefins by cytochromes P-450 and heme models: Evidence for the formation of aldehydes in addition to epoxides and allylic alcohols
    Biochemical and Biophysical Research Communications, vol. 119, no. 1, pp. 319–325, 1984
  145. Regioselectivity of olefin oxidation by iodosobenzene catalyzed by metalloporphyrins : control by the catalyst
    Tetrahedron, vol. 40, no. 15, pp. 2847–2857, 1984
  146. Reduction of benzyl halides by liver microsomes Formation of 478 nm-absorbing s-alkyl-ferric cytochrome P-450 complexes
    Biochemical Pharmacology, vol. 32, no. 12, pp. 1871–1879, 1983
  147. A heme model system for the reduction of substrates by microsomal cytochrome P 450
    Biochemical and Biophysical Research Communications, vol. 104, no. 4, pp. 1651–1657, 1982
  148. A heme model study of carbon tetrachloride metabolism: Mechanisms of phosgene and carbon dioxide formation
    Biochemical and Biophysical Research Communications, vol. 95, no. 4, pp. 1536–1542, 1980