Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase (Q36778803)

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scientific article published on 11 February 2016

Language	Label	Description	Also known as
English	Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase	scientific article published on 11 February 2016

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scholarly article

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Europe PubMed Central

PMC publication ID

16 August 2017

Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase (English)

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Europe PubMed Central

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16 August 2017

3

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12 June 2020

Beatriz Alvarez

6

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12 June 2020

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Sebastián Carballal

1

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12 June 2020

Ernesto Cuevasanta

2

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12 June 2020

Carmen Gherasim

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12 June 2020

David P Ballou

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12 June 2020

Ruma Banerjee

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12 June 2020

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publication date

11 February 2016

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16 August 2017

Journal of Biological Chemistry

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12 June 2020

291

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12 June 2020

15

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12 June 2020

8004-8013

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12 June 2020

S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase

1 reference

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Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket

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Real-time measurements of amino acid and protein hydroperoxides using coumarin boronic acid.

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NO* binds human cystathionine β-synthase quickly and tightly

1 reference

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Nitrite reductase activity and inhibition of H₂S biogenesis by human cystathionine ß-synthase

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Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite

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29 September 2017

Peroxynitrite, a stealthy biological oxidant

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4825006

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Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.

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29 September 2017

Allosteric communication between the pyridoxal 5'-phosphate (PLP) and heme sites in the H2S generator human cystathionine β-synthase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4825006

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Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions

1 reference

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Effect of the disease-causing R266K mutation on the heme and PLP environments of human cystathionine β-synthase

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Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase.

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Reversible heme-dependent regulation of human cystathionine β-synthase by a flavoprotein oxidoreductase.

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29 September 2017

Human neuroglobin functions as a redox-regulated nitrite reductase

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Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine -synthase

1 reference

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Redox biochemistry of hydrogen sulfide

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29 September 2017

Peroxynitrite is the major species formed from different flux ratios of co-generated nitric oxide and superoxide: direct reaction with boronate-based fluorescent probe

1 reference

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29 September 2017

Inactivation of cystathionine beta-synthase with peroxynitrite.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4825006

29 September 2017

Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy

1 reference

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29 September 2017

Fast ferrous heme-NO oxidation in nitric oxide synthases

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4825006

29 September 2017

Chemical biology of peroxynitrite: kinetics, diffusion, and radicals.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4825006

29 September 2017

Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation.

1 reference

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29 September 2017

The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase

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29 September 2017

Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase

1 reference

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29 September 2017

A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer

1 reference

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29 September 2017

Dynamics of carbon monoxide binding to cystathionine beta-synthase

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29 September 2017

The heme of cystathionine beta-synthase likely undergoes a thermally induced redox-mediated ligand switch

1 reference

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29 September 2017

Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control

1 reference

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29 September 2017

Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme

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Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein

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Cystathionine beta-synthase mutations in homocystinuria

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Homocysteine and cardiovascular disease

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The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations

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Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis.

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Correction to Kinetics of Reversible Reductive Carbonylation of Heme in Human Cystathionine β-Synthase

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Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions

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Ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process

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https://pubmed.ncbi.nlm.nih.gov/26867575

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Nitric Oxide Binding Properties of Neuroglobin

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Identifiers

10.1074/JBC.M116.718734

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26867575%20AND%20SRC:MED&resulttype=core&format=json

12 June 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26867575%20AND%20SRC:MED&resulttype=core&format=json

12 June 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26867575%20AND%20SRC:MED&resulttype=core&format=json

12 June 2020

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