Results 31 to 40 of about 97,911 (315)

Arabidopsis Iron Superoxide Dismutase FSD1 Protects Against Methyl Viologen-Induced Oxidative Stress in a Copper-Dependent Manner

open access: yesFrontiers in Plant Science, 2022
Iron superoxide dismutase 1 (FSD1) was recently characterized as a plastidial, cytoplasmic, and nuclear enzyme with osmoprotective and antioxidant functions. However, the current knowledge on its role in oxidative stress tolerance is ambiguous.
Pavol Melicher   +8 more
doaj   +1 more source

Mitochondrial [4Fe-4S] protein assembly involves reductive [2Fe-2S] cluster fusion on ISCA1–ISCA2 by electron flow from ferredoxin FDX2

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2020
Significance Synthesis of iron-sulfur clusters (ISC) and their insertion into apoproteins in eukaryotes requires the conserved, essential mitochondrial ISC and cytosolic Fe/S protein assembly machineries.
B. D. Weiler   +5 more
semanticscholar   +1 more source

Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction. [PDF]

open access: yes, 2020
Oxidation states of individual metal atoms within a metalloprotein can be assigned by examining X-ray absorption edges, which shift to higher energy for progressively more positive valence numbers.
Holton, James M   +3 more
core   +2 more sources

Looking for the mechanism of arsenate respiration of Fusibacter sp. strain 3D3, independent of ArrAB

open access: yesFrontiers in Microbiology, 2022
The literature has reported the isolation of arsenate-dependent growing microorganisms which lack a canonical homolog for respiratory arsenate reductase, ArrAB.
Mauricio Acosta-Grinok   +6 more
doaj   +1 more source

The interaction of ferredoxin‐linked sulfite reductase with ferredoxin [PDF]

open access: yesFEBS Letters, 1987
Spinach sulfite reductase has been shown to co‐migrate during gel filtration chromatography at low ionic strength with spinach ferredoxin. No co‐migration was observed at high ionic strength. These results indicate that the two proteins form a high‐affinity, electrostatically stabilized complex, as had previously been demonstrated for three other ...
Hirasawa, Masakazu   +4 more
openaire   +1 more source

Contribution to the Understanding of Protein–Protein Interface and Ligand Binding Site Based on Hydrophobicity Distribution—Application to Ferredoxin I and II Cases

open access: yesApplied Sciences, 2021
Ferredoxin I and II are proteins carrying a specific ligand—an iron-sulfur cluster—which allows transport of electrons. These two classes of ferredoxin in their monomeric and dimeric forms are the object of this work.
Mateusz Banach   +2 more
doaj   +1 more source

Mitochondrial De Novo Assembly of Iron–Sulfur Clusters in Mammals: Complex Matters in a Complex That Matters

open access: yesInorganics, 2022
Iron–sulfur clusters (Fe–S or ISC) are essential cofactors that function in a wide range of biological pathways. In mammalian cells, Fe–S biosynthesis primarily relies on mitochondria and involves a concerted group of evolutionary-conserved proteins ...
Tyler L. Perfitt, Alain Martelli
doaj   +1 more source

Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake [PDF]

open access: yes, 2014
The colicin-like bacteriocins are potent protein antibiotics that have evolved to efficiently cross the outer membrane of Gram-negative bacteria by parasitizing nutrient uptake systems.
Adams   +50 more
core   +3 more sources

Side chain hydroxylation of C27-steroids and vitamin D3 by a cytochrome P-450 enzyme system isolated from human liver mitochondria

open access: yesJournal of Lipid Research, 1981
The present study was undertaken to obtain information on the involvement of cytochrome P-450 in the 26-hydroxylation on bile acid intermediates and in the 25-hydroxylation of vitamin D3 in human liver mitochondria.
H Oftebro   +3 more
doaj   +1 more source

The Role of the si-Face Tyrosine of a Homodimeric Ferredoxin-NADP+ Oxidoreductase from Bacillus subtilis during Complex Formation and Redox Equivalent Transfer with NADP+/H and Ferredoxin

open access: yesAntioxidants, 2023
In the crystal structure of ferredoxin-NADP+ oxidoreductase from Bacillus subtilis (BsFNR), Tyr50 stacks on the si-face of the isoalloxazine ring portion of the FAD prosthetic group. This configuration is highly conserved among the homodimeric ferredoxin-
Daisuke Seo
doaj   +1 more source

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