30783-27-8 Usage
Explanation
The compound's full name, which describes its structure and functional groups.
Explanation
The compound belongs to the porphyrin family, which is a group of organic macrocyclic compounds with diverse applications in biology and materials science.
Explanation
The compound is a derivative of porphine, which is a simple porphyrin molecule without any substituents.
Explanation
The compound has a vinyl group (ethenyl) at the 12th position and four methyl groups at the 3rd, 8th, 13th, and 17th positions.
Explanation
The compound has three propanoic acid groups attached to the 2nd, 7th, and 18th positions of the porphyrin ring.
Explanation
Porphyrins, including this compound, are known for their role in biological processes, such as being part of the active site in hemoglobin (oxygen transport in blood) and chlorophyll (photosynthesis in plants).
Explanation
The compound can form complexes with certain metal ions and be used to selectively target cancer cells for destruction when exposed to light, making it a potential candidate for photodynamic therapy.
Explanation
Due to its unique electronic properties, the compound may have applications in the field of organic electronics.
Explanation
The molecular formula of the compound, which represents the number of carbon (C), hydrogen (H), nitrogen (N), and oxygen (O) atoms in the molecule.
Explanation
The molecular weight of the compound, which is the sum of the atomic weights of all the atoms in the molecule.
Explanation
The compound has a macrocyclic structure, which is a large ring formed by connecting multiple smaller molecules or atoms.
Explanation
The presence of carbon atoms with four different substituents (e.g., the 12th position with an ethenyl group) suggests the potential for chiral centers in the molecule, which can lead to different stereoisomers.
Family
Porphyrin
Derivative of
Porphine
Substituents
12-ethenyl, 3,8,13,17-tetramethyl
Functional Groups
Propanoic acid
Biological Role
Active site in hemoglobin and chlorophyll
Potential Application
Photodynamic therapy
Additional Application
Organic electronics
Molecular Weight
550.70 g/mol
Structure
Macrocyclic
Chirality
Potential for chiral centers
Check Digit Verification of cas no
The CAS Registry Mumber 30783-27-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,0,7,8 and 3 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 30783-27:
(7*3)+(6*0)+(5*7)+(4*8)+(3*3)+(2*2)+(1*7)=108
108 % 10 = 8
So 30783-27-8 is a valid CAS Registry Number.
30783-27-8Relevant articles and documents
Revisiting the Mechanism of the Anaerobic Coproporphyrinogen III Oxidase HemN
Ji, Xinjian,Mo, Tianlu,Liu, Wan-Qiu,Ding, Wei,Deng, Zixin,Zhang, Qi
supporting information, p. 6235 - 6238 (2019/04/04)
HemN is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the oxidative decarboxylation of coproporphyrinogen III to produce protoporphyrinogen IX, an intermediate in heme biosynthesis. HemN binds two SAM molecules in the active site, but how these two SAMs are utilized for the sequential decarboxylation of the two propionate groups of coproporphyrinogen III remains largely elusive. Provided here is evidence showing that in HemN catalysis a SAM serves as a hydrogen relay which mediates a radical-based hydrogen transfer from the propionate to the 5′-deoxyadenosyl (dAdo) radical generated from another SAM in the active site. Also observed was an unexpected shunt product resulting from trapping of the SAM-based methylene radical by the vinyl moiety of the mono-decarboxylated intermediate, harderoporphyrinogen. These results suggest a major revision of the HemN mechanism and reveal a new paradigm of the radical-mediated hydrogen transfer in radical SAM enzymology.
The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX
Rand, Katrin,Noll, Claudia,Schiebel, Hans Martin,Kemken, Dorit,Duelcks, Thomas,Kalesse, Markus,Heinz, Dirk W.,Layer, Gunhild
experimental part, p. 55 - 63 (2011/11/05)
During heme biosynthesis the oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of the two propionate side chains on rings A and B of coproporphyrinogen III to the corresponding vinyl groups to yield protoporphyrinogen IX. Here, the sequence of the two decarboxylation steps during HemN catalysis was investigated. A reaction intermediate of HemN activity was isolated by HPLC analysis and identified as monovinyltripropionic acid porphyrin by mass spectrometry. This monovinylic reaction intermediate exhibited identical chromatographic behavior during HPLC analysis as harderoporphyrin (3-vinyl-8,13,17-tripropionic acid-2,7,12,18- tetramethylporphyrin). Furthermore, HemN was able to utilize chemically synthesized harderoporphyrinogen as substrate and converted it to protoporphyrinogen IX. These results suggest that during HemN catalysis the propionate side chain of ring A of coproporphyrinogen III is decarboxylated prior to that of ring B. by Walter de Gruyter.
