Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region (Q42160152)

17 October 2017

Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region (English)

1 reference

17 October 2017

Sharp RE

1

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17 October 2017

Chapman SK

series ordinal

2

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17 October 2017

Reid GA

series ordinal

3

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17 October 2017

language of work or name

English

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publication date

1 June 1996

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17 October 2017

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17 October 2017

316 ( Pt 2)

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17 October 2017

507-513

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The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2.

17 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Intramolecular electron transfer in yeast flavocytochrome b2 upon one-electron photooxidation of the fully reduced enzyme: evidence for redox state control of heme-flavin communication

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Isolation and characterization of the flavin-binding domain of flavocytochrome b2 expressed independently in Escherichia coli

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Flavocytochrome b2 from baker's yeast. Computer-simulation studies of a new scheme for intramolecular electron transfer.

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Rapid and efficient site-specific mutagenesis without phenotypic selection

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Evidence by NMR for mobility of the cytochrome domain within flavocytochrome b2.

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

High-level expression of fully active yeast flavocytochrome b2 in Escherichia coli

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Molecular structure of flavocytochrome b2 at 2.4 A resolution

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Laser flash photolysis studies of the kinetics of electron-transfer reactions of Saccharomyces flavocytochrome b2: evidence for conformational gating of intramolecular electron transfer induced by pyruvate binding

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Tyr-143 facilitates interdomain electron transfer in flavocytochrome b2

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Flavocytochrome b2: Kinetic Studies by Absorbance and Electron-Paramagnetic-Resonance Spectroscopy of Electron Distribution among Prosthetic Groups

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Flavocytochrome b2 (Baker's yeast). Deuterium isotope effect studied by rapid-kinetic methods as a probe for the mechanism of electron transfer.

26 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Molecular Weight and Quaternary Structure of Yeast l-Lactate Dehydrogenase (Cytochrome b2). 2. Revised Heme Extinction Coefficients and Minimal Molecular Weight

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Cytochrome b2 from Bakers' Yeast (L-Lactate Dehydrogenase). A Double-Headed Enzyme

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Kinetic studies on the oxidation and reduction of the protoheme moiety of yeast L( )-lactate dehydrogenases

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems

29 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217378

Flavin to haem electron transfer in flavocytochrome b2

29 May 2018

1 reference

12 December 2020

Deletions in the interdomain hinge region of flavocytochrome b2: effects on intraprotein electron transfer

1 reference

12 December 2020

Crystalline Cytochrome b2 and Lactic Dehydrogenase of Yeast

1 reference

12 December 2020

Role of the interdomain hinge of flavocytochrome b2 in intra- and inter-protein electron transfer

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ3160507

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17 October 2017

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17 October 2017

PubMed publication ID

8687394

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