Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Asmita Singha"'
Publikováno v:
Journal of the American Chemical Society. 142:21810-21828
Phenols and quinols participate in both proton transfer and electron transfer processes in nature either in distinct elementary steps or in a concerted fashion. Recent investigations using synthetic heme/Cu models and iron porphyrins have indicated t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33089229a1f703f594f4a65bad3b8c12
https://doi.org/10.1021/jacs.0c10385
https://doi.org/10.1021/jacs.0c10385
Publikováno v:
Coordination Chemistry Reviews. 386:183-208
Heme proteins catalyse a diverse set of vital life processes using very similar heme cofactor. Thus, the inorganic chemistry community has been investigating factors in the protein active site that control their reactivity. These required synthesis o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31a3bd59c430836e8d7de834226423c7
https://doi.org/10.1016/j.ccr.2019.01.021
https://doi.org/10.1016/j.ccr.2019.01.021
Publikováno v:
Inorganica Chimica Acta. 487:63-69
The reaction of O2 with binuclear Cu(I) enzymatic active sites as well as synthetic complexes result in the formation of [Cu2O2]2 + core which can exist either in a η2η2-peroxo dicopper (II) species or bis(μ-oxo) dicopper (III) species. These spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40c79a8ded6c6731ce003b5cb58cb44d
https://doi.org/10.1016/j.ica.2018.11.026
https://doi.org/10.1016/j.ica.2018.11.026
Publikováno v:
Inorganic Chemistry. 56:3916-3925
The reaction of FeIII porphyrin complexes bearing distal hydrogen bonding residues with sulfide/hydrosulfide is kinetically monitored to reveal the presence of an intermediate and a kH/kD of 3.0. This intermediate is trapped at low temperatures and i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aea703a805c6e48ec7e0b19a71c1e7e8
https://doi.org/10.1021/acs.inorgchem.6b02878
https://doi.org/10.1021/acs.inorgchem.6b02878
Publikováno v:
Inorganic chemistry. 56(7)
The reaction of Fe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d038956d92342fff196d688bf10ea239
https://pubmed.ncbi.nlm.nih.gov/28296393
https://pubmed.ncbi.nlm.nih.gov/28296393
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 23(42)
Activation of inert C-H bonds such as those of methane are extremely challenging for chemists but in nature, the soluble methane monooxygenase (sMMO) enzyme readily oxidizes methane to methanol by using a diiron(IV) species. This has prompted chemist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d1a0b6e08e0c9e88491ce4c5c6f4995
https://pubmed.ncbi.nlm.nih.gov/28498623
https://pubmed.ncbi.nlm.nih.gov/28498623
Publikováno v:
ECS Meeting Abstracts. :427-427
Dioxygen adducts of heme proteins are ubiquitous in all O2 activating/reducing heme proteins in nature. While artificial dioxygen adducts of heme are known for six decades, till date these have not been demonstrated to be able to oxidize organic subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c56200a226f9320426462558f8cd95e
https://doi.org/10.1149/ma2019-04/9/427
https://doi.org/10.1149/ma2019-04/9/427
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 45(47)
The electronic structure and reactivity of iron porphyrin complexes bearing 2nd sphere hydrogen bonding residues have been investigated over the last few years. The presence of these weak interactions alters the spin ground state, and axial ligand bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e59665fb747ed436f6041c870043905
https://pubmed.ncbi.nlm.nih.gov/27858017
https://pubmed.ncbi.nlm.nih.gov/27858017
Autor:
Sabyasachi Bandyopadhyay, Abhishek Dey, Subhra Samanta, Atanu Rana, Asmita Singha, Kushal Sengupta, Sudipta Chatterjee, Kaustuv Mittra
Publikováno v:
Journal of inorganic biochemistry. 155
An iron porphyrin with a pre-organized hydrogen bonding (H-Bonding) distal architecture is utilized to avoid the inherent loss of entropy associated with H-Bonding from solvent (water) and mimic the behavior of metallo-enzyme active sites attributed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37d44078d916ebf2803a58e9a2aacf7a
https://pubmed.ncbi.nlm.nih.gov/26638009
https://pubmed.ncbi.nlm.nih.gov/26638009