Metal Ion Effect on the Switch of Mechanism from Direct Oxygen Transfer to Metal Ion-Coupled Electron Transfer in the Sulfoxidation of Thioanisoles by a Non-Heme Iron(IV)−Oxo Complex

2011 ◽  
Vol 133 (14) ◽  
pp. 5236-5239 ◽  
Author(s):  
Jiyun Park ◽  
Yuma Morimoto ◽  
Yong-Min Lee ◽  
Wonwoo Nam ◽  
Shunichi Fukuzumi
Keyword(s):  
Electron Transfer ◽  
Oxygen Transfer ◽  
Metal Ion ◽  
Heme Iron ◽  
Non Heme Iron

scholarly journals The oxygen reduction reaction catalyzed by Synechocystis sp. PCC 6803 flavodiiron proteins

2019 ◽  
Vol 3 (11) ◽  
pp. 3191-3200 ◽  
Author(s):  
Katherine A. Brown ◽  
Zhanjun Guo ◽  
Monika Tokmina-Lukaszewska ◽  
Liam W. Scott ◽  
Carolyn E. Lubner ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Oxygen Reduction Reaction ◽  
Oxygen Reduction ◽  
Reduction Reaction ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Mediated Electron Transfer ◽  
Synechocystis Sp ◽  
Pcc 6803

Photosynthetic flavodiiron proteins catalyze oxygen reduction at non-heme iron sites (brown spheres) using flavin (FMN) mediated electron transfer (black arrows).

Proton-Promoted Oxygen Atom Transfer vs Proton-Coupled Electron Transfer of a Non-Heme Iron(IV)-Oxo Complex

2012 ◽  
Vol 134 (8) ◽  
pp. 3903-3911 ◽  
Author(s):  
Jiyun Park ◽  
Yuma Morimoto ◽  
Yong-Min Lee ◽  
Wonwoo Nam ◽  
Shunichi Fukuzumi
Keyword(s):  
Electron Transfer ◽  
Oxygen Atom ◽  
Heme Iron ◽  
Atom Transfer ◽  
Oxygen Atom Transfer ◽  
Proton Coupled Electron Transfer ◽  
Non Heme Iron

scholarly journals Non-Transferrin-Mediated Iron Delivery

Blood ◽  
2016 ◽  
Vol 128 (22) ◽  
pp. SCI-22-SCI-22 ◽  
Author(s):  
Mitchell Knutson
Keyword(s):  
Iron Overload ◽  
Iron Metabolism ◽  
Metal Ion ◽  
Heme Iron ◽  
Iron Loading ◽  
Divalent Metal Transporter 1 ◽  
Cardiac Iron ◽  
Non Heme Iron ◽  
Juvenile Hemochromatosis ◽  
Iron Concentrations

Abstract In iron overload conditions such as thalassemia major and hereditary hemochromatosis, the iron-carrying capacity of plasma transferrin is exceeded, giving rise to non-transferrin-bound iron (NTBI). NTBI is taken up preferentially by the liver, and to a lesser extent, the kidney, pancreas, and heart. How NTBI is taken up by various tissues has been elusive. We recently demonstrated that the plasma membrane metal-ion transporter SLC39A14 (ZIP14) mediates NTBI uptake and iron loading of the liver and pancreas, but not the kidney, heart or most other tissues¹ Given that the heart is particularly susceptible to iron-related toxicity, we are currently investigating the contribution of other iron transporters to iron loading of this organ. Possible alternative cardiac iron importers include L-type and T-type calcium channels, divalent metal transporter 1 (DMT1), and SLC39A8 (ZIP8). To examine the role of DMT1 and ZIP8 in cardiac iron metabolism, we generated mice with cardiomyocyte-specific disruption of DMT1 (Dmt1heart/heart) or ZIP8 (Zip8heart/heart). The mice were then crossed with hemojuvelin knockout (Hjv-/-) mice, a model of juvenile hemochromatosis characterized by high circulating levels of NTBI. Dmt1heart/heart mice were found to have cardiac non-heme iron concentrations that were 30% lower (P<0.01) than those of wild-type littermate controls at 6 weeks of age. Interestingly, however, double mutant Hjv-/-; Dmt1heart/heart mice accumulated more cardiac non-heme iron (3.9X control) than did single-mutant Hjv-/- mice (2.3X control) at 6 weeks of age. Cardiac-specific disruption of Zip8 did not affect cardiac non-heme iron concentrations under basal conditions or when mice were crossed with Hjv-/- mice. Collectively, these data indicate that DMT1 and ZIP8 are dispensable for iron loading of the heart in a mouse model of hemochromatosis. Our data additionally suggest that DMT1 may play a role in normal cardiac iron metabolism. Reference:Jenkitkasemwong S, Wang C, Coffey R, et al. SLC39A14 is required for the development of hepatocellular iron overload in murine models of hereditary hemochromatosis.Cell Metabolism.2015; 22(1):138-150. Disclosures No relevant conflicts of interest to declare.

Effect of iron doping on protein molecular conductance

2018 ◽  
Vol 20 (20) ◽  
pp. 14072-14081 ◽  
Author(s):  
Nikolai Lebedev ◽  
Igor Griva ◽  
Anders Blom ◽  
Leonard M. Tender
Keyword(s):  
Electron Transfer ◽  
Heme Iron ◽  
Iron Doping ◽  
Non Heme Iron ◽  
Molecular Conductance

This study analyzes the role of Fe in electron transfer through non-heme iron-containing proteins.

Mechanistic Borderline of One-Step Hydrogen Atom Transfer versus Stepwise Sc3+-Coupled Electron Transfer from Benzyl Alcohol Derivatives to a Non-Heme Iron(IV)-Oxo Complex

2012 ◽  
Vol 51 (18) ◽  
pp. 10025-10036 ◽  
Author(s):  
Yuma Morimoto ◽  
Jiyun Park ◽  
Tomoyoshi Suenobu ◽  
Yong-Min Lee ◽  
Wonwoo Nam ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Hydrogen Atom ◽  
Benzyl Alcohol ◽  
Hydrogen Atom Transfer ◽  
Heme Iron ◽  
Atom Transfer ◽  
Non Heme Iron ◽  
One Step

scholarly journals Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence

2009 ◽  
Vol 390 (1) ◽  
Author(s):  
Katrin Watschinger ◽  
Markus A. Keller ◽  
Albin Hermetter ◽  
Georg Golderer ◽  
Gabriele Werner-Felmayer ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Glyceryl Ether ◽  
Metal Ion ◽  
Phenylalanine Hydroxylase ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Oxide Synthase ◽  
Aromatic Amino Acid Hydroxylases

Abstract Glyceryl ether monooxygenase is a tetrahydrobiopterin-dependent membrane-bound enzyme which catalyses the cleavage of lipid ethers into glycerol and the corresponding aldehyde. Despite many different characterisation and purification attempts, so far no gene and primary sequence have been assigned to this enzyme. The seven other tetrahydrobiopterin-dependent enzymes can be divided in the family of aromatic amino acid hydroxylases – comprising phenylalanine hydroxylase, tyrosine hydroxylase and the two tryptophan hydroxylases – and into the three nitric oxide synthases. We tested the influences of different metal ions and metal ion chelators on glyceryl ether monooxygenase, phenylalanine hydroxylase and nitric oxide synthase activity to elucidate the relationship of glyceryl ether monooxygenase to these two families. 1,10-Phenanthroline, an inhibitor of non-heme iron-dependent enzymes, was able to potently block glyceryl ether monooxygenase as well as phenylalanine hydroxylase, but had no effect on inducible nitric oxide synthase. Two tetrahydrobiopterin analogues, N5-methyltetrahydrobiopterin and 4-aminotetrahydrobiopterin, had a similar impact on glyceryl ether monooxygenase activity, as has already been shown for phenylalanine hydroxylase. These observations point to a close analogy of the role of tetrahydrobiopterin in glyceryl ether monooxygenase and in aromatic amino acid hydroxylases and suggest that glyceryl ether monooxygenase may require a non-heme iron for catalysis.

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