Results 41 to 50 of about 81,685 (258)
The iron-sulfur cluster is essential for DNA binding by human DNA polymerase ε
DNA polymerase ε (Polε) is a key enzyme for DNA replication in eukaryotes. Recently it was shown that the catalytic domain of yeast Polε (PolεCD) contains a [4Fe-4S] cluster located at the base of the processivity domain (P-domain) and coordinated by ...
Alisa E. Lisova +5 more
doaj +1 more source
Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding [PDF]
Fep1, the iron-responsive GATA factor from the methylotrophic yeast Pichia pastoris, has been characterised both in vivo and in vitro. This protein has two Cys(2)-Cys(2) type zinc fingers and a set of four conserved cysteines arranged in a Cys-X-5-Cys-X ...
Battistoni, Andrea +8 more
core +4 more sources
Functional Characterization of the Eukaryotic Cysteine Desulfurase Nfs1p from Saccharomyces cerevisiae [PDF]
Previous studies have indicated that the essential protein Nfs1 performs a crucial role in cellular iron-sulfur (Fe/S) protein maturation. The protein is located predominantly in mitochondria, yet low amounts are present in cytosol and nucleus.
Balk +73 more
core +3 more sources
Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review
Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have ...
Trnka Daniel +4 more
doaj +1 more source
Altered sterol metabolism in budding yeast affects mitochondrial iron–sulfur (Fe-S) cluster synthesis [PDF]
Ergosterol synthesis is essential for cellular growth and viability of the budding yeast Saccharomyces cerevisiae, and intracellular sterol distribution and homeostasis are therefore highly regulated in this species. Erg25 is an iron-containing C4-methyl
Bard, Martin +7 more
core +1 more source
Structural biology of ferritin nanocages
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Structures and proton-pumping strategies of mitochondrial respiratory enzymes [PDF]
Enzymes of the mitochondrial respiratory chain serve as proton pumps, using the energy made available from electron transfer reactions to transport protons across the inner mitochondrial membrane and create an electrochemical gradient used for the ...
Chan, Sunney I., Schultz, Brian E.
core +1 more source
In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai +9 more
wiley +1 more source
How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation [PDF]
During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein;
Howard, James B., Rees, Douglas C.
core +1 more source
14‐day casting‐induced immobilization reduced gastrocnemius muscle mass and increased non‐heme iron and ferritin heavy chain levels. Despite iron accumulation, transferrin receptor 1 and iron regulatory protein 2 were paradoxically upregulated. Lipid peroxidation was elevated without compensatory antioxidant responses.
Haruka Yokogawa +2 more
wiley +1 more source

