Literature DB >> 21391602

Dioxygen activation in soluble methane monooxygenase.

Christine E Tinberg1, Stephen J Lippard.   

Abstract

The controlled oxidation of methane to methanol is a chemical transformation of great value, particularly in the pursuit of alternative fuels, but the reaction remains underutilized industrially because of inefficient and costly synthetic procedures. In contrast, methane monooxygenase enzymes (MMOs) from methanotrophic bacteria achieve this chemistry efficiently under ambient conditions. In this Account, we discuss the first observable step in the oxidation of methane at the carboxylate-bridged diiron active site of the soluble MMO (sMMO), namely, the reductive activation of atmospheric O(2). The results provide benchmarks against which the dioxygen activation mechanisms of other bacterial multicomponent monooxygenases can be measured. Molecular oxygen reacts rapidly with the reduced diiron(II) cen-ter of the hydroxylase component of sMMO (MMOH). The first spectroscopically characterized intermediate that results from this process is a peroxodiiron(III) species, P*, in which the iron atoms have identical environments. P* converts to a second peroxodiiron(III) unit, H(peroxo), in a process accompanied by the transfer of a proton, probably with the assistance of a residue near the active site. Proton-promoted O-O bond scission and rearrangement of the diiron core then leads to a diiron(IV) unit, termed Q, that is directly responsible for the oxidation of methane to methanol. In one section of this Account, we provide a detailed discussion of these processes, with particular emphasis on possible structures of the intermediates. The geometries of P* and H(peroxo) are currently unknown, and recent synthetic modeling chemistry has highlighted the need for further structural characterization of Q, currently assigned as a di(μ-oxo)diiron(IV) "diamond core." In another section of the Account, we discuss in detail proton transfer during the O(2) activation events. The role of protons in promoting O-O bond cleavage, thereby initiating the conversion of H(peroxo) to Q, was previously a controversial topic. Recent studies of the mechanism, covering a range of pH values and in D(2)O instead of H(2)O, confirmed conclusively that the transfer of protons, possibly at or near the active site, is necessary for both P*-to-H(peroxo) and H(peroxo)-to-Q conversions. Specific mechanistic insights into these processes are provided. In the final section of the Account, we present our view of experiments that need to be done to further define crucial aspects of sMMO chemistry. Here our goal is to detail the challenges that we and others face in this research, particularly with respect to some long-standing questions about the system, as well as approaches that might be used to solve them.

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Year:  2011        PMID: 21391602      PMCID: PMC3079780          DOI: 10.1021/ar1001473

Source DB:  PubMed          Journal:  Acc Chem Res        ISSN: 0001-4842            Impact factor:   22.384


  44 in total

1.  Kinetics and activation thermodynamics of methane monooxygenase compound Q formation and reaction with substrates.

Authors:  B J Brazeau; J D Lipscomb
Journal:  Biochemistry       Date:  2000-11-07       Impact factor: 3.162

2.  Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters.

Authors:  Bradley J. Wallar; John D. Lipscomb
Journal:  Chem Rev       Date:  1996-11-07       Impact factor: 60.622

3.  Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases.

Authors:  Arteum D Bochevarov; Jianing Li; Woon Ju Song; Richard A Friesner; Stephen J Lippard
Journal:  J Am Chem Soc       Date:  2011-04-25       Impact factor: 15.419

4.  Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase.

Authors:  Lucas J Bailey; Brian G Fox
Journal:  Biochemistry       Date:  2009-09-29       Impact factor: 3.162

5.  Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.

Authors:  D A Whittington; A C Rosenzweig; C A Frederick; S J Lippard
Journal:  Biochemistry       Date:  2001-03-27       Impact factor: 3.162

6.  Intermediates in the oxygenation of a nonheme diiron(II) complex, including the first evidence for a bound superoxo species.

Authors:  Xiaopeng Shan; Lawrence Que
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-31       Impact factor: 11.205

7.  Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.

Authors:  Maarten Merkx; Daniel A. Kopp; Matthew H. Sazinsky; Jessica L. Blazyk; Jens Müller; Stephen J. Lippard
Journal:  Angew Chem Int Ed Engl       Date:  2001-08-03       Impact factor: 15.336

8.  Evidence for C-H cleavage by an iron-superoxide complex in the glycol cleavage reaction catalyzed by myo-inositol oxygenase.

Authors:  Gang Xing; Yinghui Diao; Lee M Hoffart; Eric W Barr; K Sandeep Prabhu; Ryan J Arner; C Channa Reddy; Carsten Krebs; J Martin Bollinger
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-10       Impact factor: 11.205

9.  Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.

Authors:  Loi H Do; Takahiro Hayashi; Pierre Moënne-Loccoz; Stephen J Lippard
Journal:  J Am Chem Soc       Date:  2010-02-03       Impact factor: 15.419

10.  Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.

Authors:  Christine E Tinberg; Stephen J Lippard
Journal:  Biochemistry       Date:  2009-12-29       Impact factor: 3.162

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  116 in total

Review 1.  Chemistry and biology of the copper chelator methanobactin.

Authors:  Grace E Kenney; Amy C Rosenzweig
Journal:  ACS Chem Biol       Date:  2011-12-12       Impact factor: 5.100

Review 2.  Architecture and active site of particulate methane monooxygenase.

Authors:  Megen A Culpepper; Amy C Rosenzweig
Journal:  Crit Rev Biochem Mol Biol       Date:  2012-06-23       Impact factor: 8.250

3.  Metalloproteins: Simple structure, complex function.

Authors:  Angela Lombardi
Journal:  Nat Chem Biol       Date:  2015-10       Impact factor: 15.040

4.  High-Resolution Extended X-ray Absorption Fine Structure Analysis Provides Evidence for a Longer Fe···Fe Distance in the Q Intermediate of Methane Monooxygenase.

Authors:  George E Cutsail; Rahul Banerjee; Ang Zhou; Lawrence Que; John D Lipscomb; Serena DeBeer
Journal:  J Am Chem Soc       Date:  2018-11-16       Impact factor: 15.419

5.  An Iron(II)(1,3-bis(2'-pyridylimino)isoindoline) Complex as a Catalyst for Substrate Oxidation with H2O2. Evidence for a Transient Peroxodiiron(III) Species.

Authors:  József S Pap; Matthew A Cranswick; E Balogh-Hergovich; Gábor Baráth; Michel Giorgi; Gregory T Rohde; József Kaizer; Gábor Speier; Lawrence Que
Journal:  Eur J Inorg Chem       Date:  2013-08       Impact factor: 2.524

6.  A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.

Authors:  Andrew J Jasniewski; Cory J Knoot; John D Lipscomb; Lawrence Que
Journal:  Biochemistry       Date:  2016-10-07       Impact factor: 3.162

Review 7.  Diiron monooxygenases in natural product biosynthesis.

Authors:  Anna J Komor; Andrew J Jasniewski; Lawrence Que; John D Lipscomb
Journal:  Nat Prod Rep       Date:  2018-07-18       Impact factor: 13.423

Review 8.  Beyond iron: non-classical biological functions of bacterial siderophores.

Authors:  Timothy C Johnstone; Elizabeth M Nolan
Journal:  Dalton Trans       Date:  2015-04-14       Impact factor: 4.390

9.  Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.

Authors:  Effie C Kisgeropoulos; Julia J Griese; Zachary R Smith; Rui M M Branca; Camille R Schneider; Martin Högbom; Hannah S Shafaat
Journal:  J Am Chem Soc       Date:  2020-03-09       Impact factor: 15.419

10.  Hydrogen-bonding effects on the reactivity of [X-Fe(III)-O-Fe(IV)═O] (X = OH, F) complexes toward C-H bond cleavage.

Authors:  Genqiang Xue; Caiyun Geng; Shengfa Ye; Adam T Fiedler; Frank Neese; Lawrence Que
Journal:  Inorg Chem       Date:  2013-03-15       Impact factor: 5.165

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