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Structures of Fe(II) Complexes with N,N,N'-Tris(2-pyridylmethyl)ethane-1,2-diamine Type Ligands. Bleomycin-like DNA Cleavage and Enhancement by an Alkylammonium Substituent on the N' Atom of the Ligand.
Mialane P, Nivorojkine A, Pratviel G, Azéma L, Slany M, Godde F, Simaan A, Banse F, Kargar-Grisel T, Bouchoux G, Sainton J, Horner O, Guilhem J, Tchertanova L, Meunier B, Girerd JJ. Mialane P, et al. Among authors: horner o. Inorg Chem. 1999 Mar 22;38(6):1085-1092. doi: 10.1021/ic971059i. Inorg Chem. 1999. PMID: 11670888
Mössbauer characterization of an unusual high-spin side-on peroxo-Fe3+ species in the active site of superoxide reductase from Desulfoarculus Baarsii. Density functional calculations on related models.
Horner O, Mouesca JM, Oddou JL, Jeandey C, Nivière V, Mattioli TA, Mathé C, Fontecave M, Maldivi P, Bonville P, Halfen JA, Latour JM. Horner O, et al. Biochemistry. 2004 Jul 13;43(27):8815-25. doi: 10.1021/bi0498151. Biochemistry. 2004. PMID: 15236590 Free article.
Superoxide reductase (SOR) is an Fe protein that catalyzes the reduction of superoxide to give H(2)O(2). Recently, the mutation of the Glu47 residue into alanine (E47A) in the active site of SOR from Desulfoarculus baarsii has allowed the stabilization of an iron-peroxo sp …
Superoxide reductase (SOR) is an Fe protein that catalyzes the reduction of superoxide to give H(2)O(2). Recently, the mutation of th …
Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase.
Horner O, Mouesca JM, Solari PL, Orio M, Oddou JL, Bonville P, Jouve HM. Horner O, et al. J Biol Inorg Chem. 2007 May;12(4):509-25. doi: 10.1007/s00775-006-0203-9. Epub 2007 Jan 20. J Biol Inorg Chem. 2007. PMID: 17237942
19 results