Results 41 to 50 of about 83,013 (204)

A [4Fe-4S] cluster resides at the active center of phosphomevalonate dehydratase, a key enzyme in the archaeal modified mevalonate pathway

open access: yesFrontiers in Microbiology, 2023
The recent discovery of the archaeal modified mevalonate pathway revealed that the fundamental units for isoprenoid biosynthesis (isopentenyl diphosphate and dimethylallyl diphosphate) are biosynthesized via a specific intermediate, trans ...
Mutsumi Komeyama   +6 more
doaj   +1 more source

FDX2, an iron-sulfur cluster assembly factor, is essential to prevent cellular senescence, apoptosis or ferroptosis of ovarian cancer cells. [PDF]

open access: goldJ Biol Chem
Miyahara S   +13 more
europepmc   +3 more sources

Low-energy spectrum of iron-sulfur clusters directly from many-particle quantum mechanics [PDF]

open access: yes, 2014
FeS clusters are a universal biological motif. They carry out electron transfer, redox chemistry, and even oxygen sensing, in diverse processes including nitrogen fixation, respiration, and photosynthesis. The low-lying electronic states are key to their
Chan, Garnet Kin-Lic   +3 more
core   +2 more sources

TusA influences Fe-S cluster assembly and iron homeostasis in E. coli by reducing the translation efficiency of Fur

open access: yesMicrobiology Spectrum
All sulfur transfer pathways have generally a l-cysteine desulfurase as an initial sulfur-mobilizing enzyme in common, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell.
Paolo Olivieri   +8 more
doaj   +1 more source

Evolutionary conservation and in vitro reconstitution of microsporidian iron–sulfur cluster biosynthesis

open access: yesNature Communications, 2017
The functions of the highly reduced mitochondria (mitosomes) of microsporidians are not well-characterized. Here, the authors show that theTrachipleistophora hominismitosome is the site of iron–sulfur cluster assembly and that its retention is likely ...
Sven-A. Freibert   +14 more
doaj   +1 more source

NsrR from Streptomyces coelicolor is a nitric oxide-sensing [4Fe-4S] cluster protein with a specialized regulatory function [PDF]

open access: yes, 2015
The Rrf2 family transcription factor NsrR controls expression of genes in a wide range of bacteria in response to nitric oxide (NO). The precise form of the NO-sensing module of NsrR is the subject of controversy because NsrR proteins containing either ...
Al-Bassam, Mahmoud   +12 more
core   +1 more source

Functional Characterization of the Eukaryotic Cysteine Desulfurase Nfs1p from Saccharomyces cerevisiae [PDF]

open access: yes, 2004
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

Genetic/metabolic effect of iron metabolism and rare anemias

open access: yesThalassemia Reports, 2013
Advances in iron metabolism have allowed a novel classification of iron disorders and to identify previously unknown diseases. These disorders include genetic iron overload (hemochromatosis) and inherited iron-related anemias, in some cases accompanied ...
Clara Camaschella
doaj   +1 more source

Structures and proton-pumping strategies of mitochondrial respiratory enzymes [PDF]

open access: yes, 2001
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

Evolutionary cell biology: Functional insight from “Endless forms most beautiful” [PDF]

open access: yes, 2015
In animal and fungal model organisms, the complexities of cell biology have been analyzed in exquisite detail and much is known about how these organisms function at the cellular level.
Dacks, Joel B.   +4 more
core   +1 more source

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