Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase (Q35040660)

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English	Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 August 2017

Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase (English)

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Carsten Krebs

5

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J. Martin Bollinger Jr.

6

object named as

J Martin Bollinger

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Europe PubMed Central

PubMed publication ID

6 August 2017

author name string

Ning Li

1

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6 August 2017

Hanne Nørgaard

2

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6 August 2017

Douglas M Warui

3

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6 August 2017

Squire J Booker

4

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6 August 2017

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publication date

4 April 2011

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6 August 2017

Journal of the American Chemical Society

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6 August 2017

133

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Europe PubMed Central

PubMed publication ID

6 August 2017

16

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Europe PubMed Central

PubMed publication ID

6 August 2017

6158-6161

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Europe PubMed Central

PubMed publication ID

6 August 2017

Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Engineering cyanobacteria to generate high-value products

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

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Ferric Superoxide and Ferric Hydroxide Are Used in the Catalytic Mechanism of Hydroxyethylphosphonate Dioxygenase: A Density Functional Theory Investigation

1 reference

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Synthesis, structural, and spectroscopic characterization and reactivities of mononuclear cobalt(III)-peroxo complexes

1 reference

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Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus

1 reference

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Geometric and electronic structure and reactivity of a mononuclear "side-on" nickel(III)-peroxo complex

1 reference

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A tyrosyl-dimanganese coupled spin system is the native metalloradical cofactor of the R2F subunit of the ribonucleotide reductase of Corynebacterium ammoniagenes

1 reference

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Microbial Biosynthesis of Alkanes

1 reference

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Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer

1 reference

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An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.

1 reference

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8 July 2018

Insights into the (superoxo)Fe(III)Fe(III) intermediate and reaction mechanism of myo-inositol oxygenase: DFT and ONIOM(DFT:MM) study

1 reference

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8 July 2018

A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus

1 reference

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8 July 2018

Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Characterization of the arene-oxidizing intermediate in ToMOH as a diiron(III) species

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Di-iron-tyrosyl radical ribonucleotide reductases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

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.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Di-iron-carboxylate proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme.

1 reference

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8 July 2018

Three-dimensional structure of the free radical protein of ribonucleotide reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

Nature of the free radical in ribonucleotide reductase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3113487

8 July 2018

YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase.

1 reference

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25 October 2018

(Mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse.

1 reference

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The reactivity of well defined diiron(III) peroxo complexes toward substrates: addition to electrophiles and hydrocarbon oxidation

1 reference

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1 reference

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Reactions of the diiron enzyme stearoyl-acyl carrier protein desaturase

1 reference

https://pubmed.ncbi.nlm.nih.gov/21462983

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Mononuclear nonheme ferric-peroxo complex in aldehyde deformylation

1 reference

https://pubmed.ncbi.nlm.nih.gov/21462983

12 December 2020

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Structural characterization and remarkable axial ligand effect on the nucleophilic reactivity of a nonheme manganese(III)-peroxo complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/21462983

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Biofuels. ExxonMobil fuels Venter's efforts to run vehicles on algae-based oil

1 reference

https://pubmed.ncbi.nlm.nih.gov/21462983

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Ribonucleotide reductases

1 reference

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Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/21462983

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/JA2013517

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Europe PubMed Central

PubMed publication ID

6 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

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