859-38-1 Usage
Molecular structure
1H-Pyrrole-3-propanoic acid, 2-[(acetyloxy)methyl]-4-methyl-5-[(phenylmethoxy)carbonyl]-, methyl ester is a complex organic compound that consists of a pyrrole ring, a propanoic acid group, an ester group, an acetyloxy group, and a phenylmethoxy carbonyl group.
Functional groups
The compound contains multiple functional groups, including a pyrrole ring, a propanoic acid group, an ester group, an acetyloxy group, and a phenylmethoxy carbonyl group.
Reactivity
The compound's unique combination of functional groups and structural characteristics give it specific properties and reactivity, making it a valuable building block for the synthesis of more complex molecules.
Applications
1H-Pyrrole-3-propanoic acid, 2-[(acetyloxy)methyl]-4-methyl-5-[(phenylmethoxy)carbonyl]-, methyl ester has potential applications in various fields, including organic synthesis, pharmaceuticals, and materials science.
Pharmaceutical potential
The compound's potential pharmaceutical applications make it an interesting target for further research and development.
Check Digit Verification of cas no
The CAS Registry Mumber 859-38-1 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 8,5 and 9 respectively; the second part has 2 digits, 3 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 859-38:
(5*8)+(4*5)+(3*9)+(2*3)+(1*8)=101
101 % 10 = 1
So 859-38-1 is a valid CAS Registry Number.
859-38-1Relevant articles and documents
Corrole-Substituted Fluorescent Heme Proteins
Lemon, Christopher M.,Marletta, Michael A.
, p. 2716 - 2729 (2021)
Although fluorescent proteins have been utilized for a variety of biological applications, they have several optical limitations, namely weak red and near-infrared emission and exceptionally broad (>200 nm) emission profiles. The photophysical properties of fluorescent proteins can be enhanced through the incorporation of novel cofactors with the desired properties into a stable protein scaffold. To this end, a fluorescent phosphorus corrole that is structurally similar to the native heme cofactor is incorporated into two exceptionally stable heme proteins: H-NOX from Caldanaerobacter subterraneus and heme acquisition system protein A (HasA) from Pseudomonas aeruginosa. These yellow-orange emitting protein conjugates are examined by steady-state and time-resolved optical spectroscopy. The HasA conjugate exhibits enhanced fluorescence, whereas emission from the H-NOX conjugate is quenched relative to the free corrole. Despite the low fluorescence quantum yields, these corrole-substituted proteins exhibit more intense fluorescence in a narrower spectral profile than traditional fluorescent proteins that emit in the same spectral window. This study demonstrates that fluorescent corrole complexes are readily incorporated into heme proteins and provides an inroad for the development of novel fluorescent proteins.
