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H17082

Sigma-Aldrich

2-Hydrazinopyridine

97%

Synonyme(s) :

2-Pyridylhydrazine

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About This Item

Formule empirique (notation de Hill):
C5H7N3
Numéro CAS:
4930-98-7
Poids moléculaire :
109.13
Numéro Beilstein :
109984
Numéro CE :
225-566-8
Numéro MDL:
MFCD00006249
Code UNSPSC :
12352100
ID de substance PubChem :
24895475
Nomenclature NACRES :
NA.22

Pureté

97%

Point d'ébullition

90-92 °C/1 mmHg (lit.)

Pf

41-44 °C (lit.)

Température de stockage

2-8°C

Chaîne SMILES 

NNc1ccccn1

InChI

1S/C5H7N3/c6-8-5-3-1-2-4-7-5/h1-4H,6H2,(H,7,8)

Clé InChI

NWELCUKYUCBVKK-UHFFFAOYSA-N

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Catégories apparentées

Application

  • Enhanced Metal Removal: Utilizing Schiff base functionalized dialdehyde starch, derived from 2-hydrazinopyridine, demonstrated significant potential in enhancing the removal of Cu(II) from solutions. The study included preparation methodologies, performance evaluations, and DFT calculations, showcasing its efficacy in water treatment technologies (Liang et al., 2024).
  • Dual Sensing Probe Development: A novel dicyanisophorone-based probe, incorporating 2-hydrazinopyridine, was developed for the dual sensing of Zn(2+) and Cd(2+) via near-infrared fluorescence. This advancement aids in the detection and analysis of heavy metals in various environmental and biological samples (Yan et al., 2023).
  • Active Site Analysis in Lysyl Oxidase: The study provided insights into the spatial arrangement of active site components in Lysyl Oxidase-like 2, including the role of 2-hydrazinopyridine, which is critical for understanding the enzyme′s mechanism and potential therapeutic applications (Meier et al., 2022).
  • Structural Analysis of Lysyl Oxidase: Research focused on the predicted 3D structure of the amine oxidase domain of Lysyl Oxidase-Like 2, exploring the interaction dynamics facilitated by 2-hydrazinopyridine. This contributes significantly to the field of molecular biology and enzyme function analysis (Meier et al., 2022).

Pictogrammes

Exclamation mark
GHS07

Mention d'avertissement

Warning

Mentions de danger

H315,H319,H335

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

230.0 °F - closed cup

Point d'éclair (°C)

110 °C - closed cup

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves

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Minae Mure et al.
Biochemistry, 44(5), 1583-1594 (2005-02-03)
Adduct I (lambda(max) at approximately 430 nm) formed in the reaction of 2-hydrazinopyridine (2HP) and the TPQ cofactor of wild-type Escherichia coli copper amine oxidase (WT-ECAO) is stable at neutral pH, 25 degrees C, but slowly converts to another spectroscopically
P Knowles et al.
Journal of neural transmission (Vienna, Austria : 1996), 114(6), 743-746 (2007-04-05)
Tranylcypromine (TCP), an amphetamine, is a reversible inhibitor of copper-containing amine oxidases. We have solved the structure of the complex of TCP with the amine oxidase from E. coli (ECAO) and shown that only the (+)-enantiomer of TCP binds. Kinetic
Christian R P Kurtis et al.
Journal of neural transmission (Vienna, Austria : 1996), 118(7), 1043-1053 (2011-05-07)
Copper amine oxidases are important for the metabolism of a range of biogenic amines. Here, we focus on substrate specificity in the E. coli copper amine oxidase (ECAO) and specifically the role of Tyr 381. This residue, and its equivalent
Minae Mure et al.
Biochemistry, 44(5), 1568-1582 (2005-02-03)
2-Hydrazinopyridine (2HP) is an irreversible inhibitor of copper amine oxidases (CAOs). 2HP reacts directly at the C5 position of the TPQ cofactor, yielding an intense chromophore with lambda(max) approximately 430 nm (adduct I) in Escherichia coli amine oxidase (ECAO). The
Emma Jakobsson et al.
Acta crystallographica. Section D, Biological crystallography, 61(Pt 11), 1550-1562 (2005-10-22)
Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs). SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process. The structure
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