A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical (Q36735315)

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English	A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical	scholarly article

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scholarly article

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Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

title

A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical (English)

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Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

author

Aimin Liu

object named as

Aimin Liu

series ordinal

6

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Carsten Krebs

object named as

Carsten Krebs

series ordinal

4

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Victor L. Davidson

object named as

Victor L Davidson

series ordinal

5

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author name string

Xianghui Li

series ordinal

1

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Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

Rong Fu

series ordinal

2

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stated in

Europe PubMed Central

PMC publication ID

2438432

retrieved

16 August 2017

Sheeyong Lee

series ordinal

3

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stated in

Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

language of work or name

English

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publication date

18 June 2008

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Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

published in

Proceedings of the National Academy of Sciences of the United States of America

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stated in

Europe PubMed Central

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2438432

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16 August 2017

volume

105

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stated in

Europe PubMed Central

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2438432

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16 August 2017

issue

25

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Europe PubMed Central

PMC publication ID

2438432

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16 August 2017

page(s)

8597-8600

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PMC publication ID

2438432

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16 August 2017

cites work

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Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation

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Heme-Containing Oxygenases

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Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase

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Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides.

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Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution

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Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis

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Mutational Analysis of Mau Genes Involved in Methylamine Metabolism in Paracoccus Denitrificans

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Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase

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MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis

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MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase

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Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue.

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Control of electronic structure of a six-coordinate iron(III) porphyrin radical by means of axial ligands

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Mechanistic Possibilities in MauG-Dependent Tryptophan Tryptophylquinone Biosynthesis†

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21 January 2018

An Fe2IVO2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase

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21 January 2018

EPR and ENDOR detection of compound I from Micrococcus lysodeikticus catalase

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Mössbauer effect in peroxidase

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Escherichia coli ribonucleotide reductase. Radical susceptibility to hydroxyurea is dependent on the regulatory state of the enzyme

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Mössbauer Characterization of Paracoccus denitrificans Cytochrome c Peroxidase

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Moessbauer and electron paramagnetic resonance studies of horseradish peroxidase and its catalytic intermediates

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/18562294

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18562294

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein Radicals in Enzyme Catalysis

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18562294

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based on heuristic

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The detection of two electron paramagnetic resonance radical signals associated with chloroperoxidase compound I

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/18562294

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.0801643105

1 reference

stated in

Europe PubMed Central

PMC publication ID

2438432

retrieved

16 August 2017

ADS bibcode

2008PNAS..105.8597L

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PMC publication ID

2438432

1 reference

stated in

Europe PubMed Central

PMC publication ID

2438432

retrieved

16 August 2017

PubMed publication ID

18562294

1 reference

stated in

Europe PubMed Central

PMC publication ID

2438432

retrieved

16 August 2017

ResearchGate publication ID

5292996

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