Dataset Information

A Non-Heme Iron Photocatalyst for Light-Driven Aerobic Oxidation of Methanol.

ABSTRACT: Non-heme (L)FeIII and (L)FeIII -O-FeIII (L) complexes (L=1,1-di(pyridin-2-yl)-N,N-bis(pyridin-2-ylmethyl)ethan-1-amine) underwent reduction under irradiation to the FeII state with concomitant oxidation of methanol to methanal, without the need for a secondary photosensitizer. Spectroscopic and DFT studies support a mechanism in which irradiation results in charge-transfer excitation of a FeIII -?-O-FeIII complex to generate [(L)FeIV =O]2+ (observed transiently during irradiation in acetonitrile), and an equivalent of (L)FeII . Under aerobic conditions, irradiation accelerates reoxidation from the FeII to the FeIII state with O2 , thus closing the cycle of methanol oxidation to methanal.

SUBMITTER: Chen J

PROVIDER: S-EPMC5887871 | biostudies-other | 2018 Mar

REPOSITORIES: biostudies-other

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A Non-Heme Iron Photocatalyst for Light-Driven Aerobic Oxidation of Methanol.

Chen Juan J Stepanovic Stepan S Draksharapu Apparao A Gruden Maja M Browne Wesley R WR

Angewandte Chemie (International ed. in English) 20180219 12

Non-heme (L)FeIII and (L)FeIII -O-FeIII (L) complexes (L=1,1-di(pyridin-2-yl)-N,N-bis(pyridin-2-ylmethyl)ethan-1-amine) underwent reduction under irradiation to the FeII state with concomitant oxidation of methanol to methanal, without the need for a secondary photosensitizer. Spectroscopic and DFT studies support a mechanism in which irradiation results in charge-transfer excitation of a FeIII -μ-O-FeIII complex to generate [(L)F ...[more]

PMID: 29334586

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Project description:BackgroundHeme and non-heme iron from diet, and recycled iron from hemoglobin are important products of the synthesis of iron-containing molecules. In excess, iron is potentially toxic because it can produce reactive oxygen species through the Fenton reaction. Humans can absorb, transport, store, and recycle iron without an excretory system to remove excess iron. Two candidate heme transporters and two iron transporters have been reported thus far. Heme incorporated into cells is degraded by heme oxygenases (HOs), and the iron product is reutilized by the body. To specify the processes of heme uptake and degradation, and the reutilization of iron, we determined the subcellular localizations of these transporters and HOs.ResultsIn this study, we analyzed the subcellular localizations of 2 isoenzymes of HOs, 4 isoforms of divalent metal transporter 1 (DMT1), and 2 candidate heme transporters--heme carrier protein 1 (HCP1) and heme responsive gene-1 (HRG-1)--in non-polarized and polarized cells. In non-polarized cells, HCP1, HRG-1, and DMT1A-I are located in the plasma membrane. In polarized cells, they show distinct localizations: HCP1 and DMT1A-I are located in the apical membrane, whereas HRG-1 is located in the basolateral membrane and lysosome. 16Leu at DMT1A-I N-terminal cytosolic domain was found to be crucial for plasma membrane localization. HOs are located in smooth endoplasmic reticulum and colocalize with NADPH-cytochrome P450 reductase.ConclusionsHCP1 and DMT1A-I are localized to the apical membrane, and HRG-1 to the basolateral membrane and lysosome. These findings suggest that HCP1 and DMT1A-I have functions in the uptake of dietary heme and non-heme iron. HRG-1 can transport endocytosed heme from the lysosome into the cytosol. These localization studies support a model in which cytosolic heme can be degraded by HOs, and the resulting iron is exported into tissue fluids via the iron transporter ferroportin 1, which is expressed in the basolateral membrane in enterocytes or in the plasma membrane in macrophages. The liberated iron is transported by transferrin and reutilized for hemoglobin synthesis in the erythroid system.

Dataset Information

A Non-Heme Iron Photocatalyst for Light-Driven Aerobic Oxidation of Methanol.

Publications

A Non-Heme Iron Photocatalyst for Light-Driven Aerobic Oxidation of Methanol.

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