Literature DB >> 9461283

The 2-His-1-carboxylate facial triad--an emerging structural motif in mononuclear non-heme iron(II) enzymes.

E L Hegg1, L Que.   

Abstract

A 2-His-1-carboxylate facial triad is a common feature of the active sites in a number of mononuclear non-heme iron(II) enzymes. This structural motif was established crystallographically for five different classes of enzymes and inferred from sequence similarity for two other classes. The 2-His-1-carboxylate facial triad anchors the iron in the active site and at the same time maintains three additional cis-oriented sites. These sites can be used to bind other endogenous ligands or exogenous ligands such as substrate and/or O2, giving the metal center great flexibility to use different mechanistic strategies to perform a variety of chemical transformations.

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Year:  1997        PMID: 9461283     DOI: 10.1111/j.1432-1033.1997.t01-1-00625.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  134 in total

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Review 3.  Mechanism of aromatic amino acid hydroxylation.

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Review 4.  The role of active-site residues in naphthalene dioxygenase.

Authors:  Rebecca E Parales
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Review 5.  Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.

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Journal:  J Biol Inorg Chem       Date:  2017-01-13       Impact factor: 3.358

6.  Calorimetric assessment of Fe(2+) binding to α-ketoglutarate/taurine dioxygenase: ironing out the energetics of metal coordination by the 2-His-1-carboxylate facial triad.

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Journal:  Inorg Chem       Date:  2015-02-10       Impact factor: 5.165

7.  Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.

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8.  Metal ions-stimulated iron oxidation in hydroxylases facilitates stabilization of HIF-1 alpha protein.

Authors:  Monika Kaczmarek; Raul E Cachau; Igor A Topol; Kazimierz S Kasprzak; Andy Ghio; Konstantin Salnikow
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9.  An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.

Authors:  Fange Liu; Jiafeng Geng; Ryan H Gumpper; Arghya Barman; Ian Davis; Andrew Ozarowski; Donald Hamelberg; Aimin Liu
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10.  Fe(II)/alpha-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism.

Authors:  Jana M Simmons; Tina A Müller; Robert P Hausinger
Journal:  Dalton Trans       Date:  2008-06-27       Impact factor: 4.390

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