Literature DB >> 19007887

Mechanism of extradiol aromatic ring-cleaving dioxygenases.

John D Lipscomb1.   

Abstract

The extradiol aromatic ring-cleaving dioxygenases activate molecular oxygen by binding both O(2) and the catecholic substrate to a reduced active site metal, generally Fe(II). Progress has been made in understanding the mechanism of this reaction through the combined use of kinetic, computational, biomimetic, structural, and diagnostic chemical approaches. It appears that O(2) is activated by accepting an electron transferred from the substrate through the metal, thereby simultaneously activating oxygen and substrate for reaction with each other.

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Year:  2008        PMID: 19007887      PMCID: PMC2614828          DOI: 10.1016/j.sbi.2008.11.001

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  38 in total

Review 1.  Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates.

Authors:  Miquel Costas; Mark P Mehn; Michael P Jensen; Lawrence Que
Journal:  Chem Rev       Date:  2004-02       Impact factor: 60.622

2.  Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7-triazacyclononane: insight into the mechanism of the extradiol catechol dioxygenases.

Authors:  G Lin; G Reid; T D Bugg
Journal:  J Am Chem Soc       Date:  2001-05-30       Impact factor: 15.419

3.  Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.

Authors:  Andreas Karlsson; Juanito V Parales; Rebecca E Parales; David T Gibson; Hans Eklund; S Ramaswamy
Journal:  Science       Date:  2003-02-14       Impact factor: 47.728

4.  Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography.

Authors:  Frédéric H Vaillancourt; Christopher J Barbosa; Thomas G Spiro; Jeffrey T Bolin; Michael W Blades; Robin F B Turner; Lindsay D Eltis
Journal:  J Am Chem Soc       Date:  2002-03-20       Impact factor: 15.419

Review 5.  Quantum chemical studies of dioxygen activation by mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad.

Authors:  Arianna Bassan; Tomasz Borowski; Per E M Siegbahn
Journal:  Dalton Trans       Date:  2004-08-27       Impact factor: 4.390

6.  Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase.

Authors:  Nobuyuki Sato; Yoshitaka Uragami; Tomoko Nishizaki; Yoshito Takahashi; Gen Sazaki; Keisuke Sugimoto; Takamasa Nonaka; Eiji Masai; Masao Fukuda; Toshiya Senda
Journal:  J Mol Biol       Date:  2002-08-23       Impact factor: 5.469

7.  Evidence from mechanistic probes for distinct hydroperoxide rearrangement mechanisms in the intradiol and extradiol catechol dioxygenases.

Authors:  Meite Xin; Timothy D H Bugg
Journal:  J Am Chem Soc       Date:  2008-07-16       Impact factor: 15.419

8.  Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases.

Authors:  Per E M Siegbahn; Fredrik Haeffner
Journal:  J Am Chem Soc       Date:  2004-07-28       Impact factor: 15.419

9.  A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases.

Authors:  Robert J Deeth; Timothy D H Bugg
Journal:  J Biol Inorg Chem       Date:  2003-02-11       Impact factor: 3.358

10.  Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.

Authors:  Matthew W Vetting; Lawrence P Wackett; Lawrence Que; John D Lipscomb; Douglas H Ohlendorf
Journal:  J Bacteriol       Date:  2004-04       Impact factor: 3.490

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  64 in total

1.  In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase.

Authors:  Erik R Farquhar; Joseph P Emerson; Kevin D Koehntop; Mark F Reynolds; Milena Trmčić; Lawrence Que
Journal:  J Biol Inorg Chem       Date:  2011-01-30       Impact factor: 3.358

2.  Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains.

Authors:  Fernando Gandía-Herrero; Francisco García-Carmona
Journal:  Planta       Date:  2012-01-24       Impact factor: 4.116

Review 3.  Microbial degradation of aromatic compounds - from one strategy to four.

Authors:  Georg Fuchs; Matthias Boll; Johann Heider
Journal:  Nat Rev Microbiol       Date:  2011-10-03       Impact factor: 60.633

4.  A preliminary crystallographic study of recombinant NicX, an Fe(2+)-dependent 2,5-dihydroxypyridine dioxygenase from Pseudomonas putida KT2440.

Authors:  José Ignacio Jiménez; Iván Acebrón; José Luis García; Eduardo Díaz; José Miguel Mancheño
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-04-29

Review 5.  Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.

Authors:  Yifan Wang; Jiasong Li; Aimin Liu
Journal:  J Biol Inorg Chem       Date:  2017-01-13       Impact factor: 3.358

Review 6.  Ring-cleaving dioxygenases with a cupin fold.

Authors:  Susanne Fetzner
Journal:  Appl Environ Microbiol       Date:  2012-01-27       Impact factor: 4.792

7.  Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate Dioxygenase.

Authors:  Brent S Rivard; Melanie S Rogers; Daniel J Marell; Matthew B Neibergall; Sarmistha Chakrabarty; Christopher J Cramer; John D Lipscomb
Journal:  Biochemistry       Date:  2015-07-21       Impact factor: 3.162

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

Authors:  Yifan Wang; Kathy Fange Liu; Yu Yang; Ian Davis; Aimin Liu
Journal:  Proc Natl Acad Sci U S A       Date:  2020-07-30       Impact factor: 11.205

9.  Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant.

Authors:  Michael M Mbughuni; Katlyn K Meier; Eckard Münck; John D Lipscomb
Journal:  Biochemistry       Date:  2012-10-29       Impact factor: 3.162

10.  Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation.

Authors:  Elena G Kovaleva; John D Lipscomb
Journal:  Biochemistry       Date:  2012-10-29       Impact factor: 3.162

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