A new mononuclear Fe(iii) Mannich-base complex with selective histidine binding and catechol oxidase activity. (13th February 2023)
- Record Type:
- Journal Article
- Title:
- A new mononuclear Fe(iii) Mannich-base complex with selective histidine binding and catechol oxidase activity. (13th February 2023)
- Main Title:
- A new mononuclear Fe(iii) Mannich-base complex with selective histidine binding and catechol oxidase activity
- Authors:
- Mandal, Bikramaditya
Haldar, Anwesha
Ganguly, Rakesh
Saha, Rajat
Mandal, Debdas - Abstract:
- Abstract : The design of amino acid sensors have significant applications in biomarkers. Abstract : The design of amino acid sensors have significant applications in biomarkers. Herein, we have developed an achiral Fe(iii )-complex [Fe III L(bzac)] (complex 1 ) (H2 L = N, N ′-dimethyl- N, N ′-bi(2-hydroxy-3, 5-dichlorobenzyl)-ethylenediamine (H2 L ) that shows highly selective sensing of histidine over others in an aqueous methanolic solution. The complex has been synthesized by a simple stirring method using H2 L and benzylacetone (bzac) as the ancillary ligand and characterized by single crystal X-ray diffraction analysis along with other spectroscopic studies. Structural study shows that it is a simple mononuclear complex though the single molecule is chiral; however, the overall crystalline lattice is achiral in nature. In the complex, Fe(iii ) shows distorted octahedral geometry, and each discrete complex is connected by supramolecular hydrogen bonding interactions to form achiral 3D supramolecular structure. Both the absorption spectral analyses reveal that the complex has peaks at 484 nm due to ligand-to-metal charge transfer (LMCT) and emission spectra have a peak at 566 nm. In the presence of histidine, there is a red-shift of about 70 nm and peaks arise at about 564 nm, while the emission spectra shows that the peak at 566 nm disappears completely and a new peak at 603 nm appears. In the presence of other amino acids, there is no such distinct change in both theAbstract : The design of amino acid sensors have significant applications in biomarkers. Abstract : The design of amino acid sensors have significant applications in biomarkers. Herein, we have developed an achiral Fe(iii )-complex [Fe III L(bzac)] (complex 1 ) (H2 L = N, N ′-dimethyl- N, N ′-bi(2-hydroxy-3, 5-dichlorobenzyl)-ethylenediamine (H2 L ) that shows highly selective sensing of histidine over others in an aqueous methanolic solution. The complex has been synthesized by a simple stirring method using H2 L and benzylacetone (bzac) as the ancillary ligand and characterized by single crystal X-ray diffraction analysis along with other spectroscopic studies. Structural study shows that it is a simple mononuclear complex though the single molecule is chiral; however, the overall crystalline lattice is achiral in nature. In the complex, Fe(iii ) shows distorted octahedral geometry, and each discrete complex is connected by supramolecular hydrogen bonding interactions to form achiral 3D supramolecular structure. Both the absorption spectral analyses reveal that the complex has peaks at 484 nm due to ligand-to-metal charge transfer (LMCT) and emission spectra have a peak at 566 nm. In the presence of histidine, there is a red-shift of about 70 nm and peaks arise at about 564 nm, while the emission spectra shows that the peak at 566 nm disappears completely and a new peak at 603 nm appears. In the presence of other amino acids, there is no such distinct change in both the absorption and emission spectra of the complex. It also acts as an effective catalyst toward the oxidation of 3, 5-di- tert -butylcatechol in methanol solvent. … (more)
- Is Part Of:
- New journal of chemistry. Volume 47:Number 10(2023)
- Journal:
- New journal of chemistry
- Issue:
- Volume 47:Number 10(2023)
- Issue Display:
- Volume 47, Issue 10 (2023)
- Year:
- 2023
- Volume:
- 47
- Issue:
- 10
- Issue Sort Value:
- 2023-0047-0010-0000
- Page Start:
- 4698
- Page End:
- 4706
- Publication Date:
- 2023-02-13
- Subjects:
- Chemistry -- Periodicals
Chimie -- Périodiques
540 - Journal URLs:
- http://www.rsc.org/ ↗
http://www.rsc.org/is/journals/current/newjchem/njc.htm ↗ - DOI:
- 10.1039/d2nj03501d ↗
- Languages:
- English
- ISSNs:
- 1144-0546
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6084.319900
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 26102.xml