Characterization of NO binding to human cystathionine beta-synthase: possible implications of the effects of CO and NO binding to the human enzyme (Q43823323)

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scientific article published in December 2001

Language	Label	Description	Also known as
English	Characterization of NO binding to human cystathionine beta-synthase: possible implications of the effects of CO and NO binding to the human enzyme	scientific article published in December 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

Characterization of NO binding to human cystathionine beta-synthase: possible implications of the effects of CO and NO binding to the human enzyme (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

author name string

Taoka S

1

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Europe PubMed Central

PubMed publication ID

27 November 2017

Banerjee R

2

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Europe PubMed Central

PubMed publication ID

27 November 2017

language of work or name

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based on heuristic

inferred from title

publication date

1 December 2001

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Europe PubMed Central

PubMed publication ID

27 November 2017

Journal of Inorganic Biochemistry

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Europe PubMed Central

PubMed publication ID

27 November 2017

87

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Europe PubMed Central

PubMed publication ID

27 November 2017

4

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Europe PubMed Central

PubMed publication ID

27 November 2017

245-251

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Europe PubMed Central

PubMed publication ID

27 November 2017

Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450.

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Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells

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Neural-tube defects and derangement of homocysteine metabolism

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Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity

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Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein

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Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation

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Functional properties of the active core of human cystathionine beta-synthase crystals.

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Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum

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Characterization of the heme in human cystathionine beta-synthase by X-ray absorption and electron paramagnetic resonance spectroscopies

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Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme

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Redox-controlled Ligand Exchange of the Heme in the CO-sensing Transcriptional Activator CooA

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Structure of the CO sensing transcription activator CooA

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Characterization of variants altered at the N-terminal proline, a novel heme-axial ligand in CooA, the CO-sensing transcriptional activator

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Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme

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Assignment of enzymatic functions to specific regions of the PLP-dependent heme protein cystathionine beta-synthase

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Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences

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Characterization of the heme and pyridoxal phosphate cofactors of human cystathionine beta-synthase reveals nonequivalent active sites

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"NONOates" (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: convenient nitric oxide dosage forms

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Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme

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Identifiers

10.1016/S0162-0134(01)00335-X

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 November 2017

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