(Q43564091)

English

alpha Arg-237 in Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein affords approximately 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone

scientific article published on 2 April 2001

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

alpha Arg-237 in Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein affords approximately 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

1 reference

based on heuristic

inferred from title

author name string

Talfournier F

1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Munro AW

2

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Basran J

3

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Sutcliffe MJ

4

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Daff S

5

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Chapman SK

6

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Scrutton NS

7

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

language of work or name

0 references

publication date

2 April 2001

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

276

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

23

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

20190-20196

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

The fix Escherichia coli region contains four genes related to carnitine metabolism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Genetic and structural analysis of the Rhizobium meliloti fixA, fixB, fixC, and fixX genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Electron-transferring flavoprotein has an AMP-binding site in addition to the FAD-binding site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Structural and redox relationships between Paracoccus denitrificans, porcine and human electron-transferring flavoproteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Electron transfer flavoprotein from Methylophilus methylotrophus: properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Unusual redox properties of electron-transfer flavoprotein from Methylophilus methylotrophus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Microcoulometric analysis of trimethylamine dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Redox control of the catalytic cycle of flavocytochrome P-450 BM3.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Natural engineering principles of electron tunnelling in biological oxidation-reduction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

The midpoint potentials for the oxidized-semiquinone couple for Gly57 mutants of the Clostridium beijerinckii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N(5) of the reduced flavin mononucleotide cofactor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: thermodynamic properties and crystal structures of glycine-61 mutants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the st

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

The functions of the flavin contact residues, alphaArg249 and betaTyr16, in human electron transfer flavoprotein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Differential Stabilization of the Three FMN Redox Forms by Tyrosine 94 and Tryptophan 57 in Flavodoxin fromAnabaenaand Its Influence on the Redox Potentials†

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Purification and properties of electron-transferring flavoprotein from pig kidney

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Formation of W(3)A(1) electron-transferring flavoprotein (ETF) hydroquinone in the trimethylamine dehydrogenase x ETF protein complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

X-ray scattering studies of Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein. Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

An exposed tyrosine on the surface of trimethylamine dehydrogenase facilitates electron transfer to electron transferring flavoprotein: kinetics of transfer in wild-type and mutant complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Crystallization and preliminary crystallographic investigation of electron-transfer flavoprotein from the bacterium Methylophilus W3A1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

On the effect of temperature on the absorption spectra of free and protein-bound flavines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Conformational energetics of a reverse turn in the Clostridium beijerinckii flavodoxin is directly coupled to the modulation of its oxidation-reduction potentials

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010853200

21 January 2018

Identifiers

10.1074/JBC.M010853200

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

release_hoy4rqd2djbzbavfkgsc6fehoq

1 reference

https://api.fatcat.wiki/v0/release/hoy4rqd2djbzbavfkgsc6fehoq

24 November 2022

based on heuristic

mapped directly with Wikidata item

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q43564091&oldid=2101121931"