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Biophysical Characterization of Iron-Sulfur Proteins [PDF]

open access: yesBio-Protocol, 2021
Iron-sulfur proteins are primordial catalysts and biological electron carriers that today drive major metabolic pathways across all forms of life. They can access a diversity of oxidation states and can mediate electron transfer over an extended range of
Bhanu Jagilinki   +4 more
doaj   +4 more sources

Bacterial Approaches for Assembling Iron-Sulfur Proteins [PDF]

open access: yesmBio, 2021
Building iron-sulfur (Fe-S) clusters and assembling Fe-S proteins are essential actions for life on Earth. The three processes that sustain life, photosynthesis, nitrogen fixation, and respiration, require Fe-S proteins.
Karla Esquilin-Lebron   +3 more
doaj   +2 more sources

Structure-function relationships of the Mycobacterium tuberculosis transcription factor WhiB1. [PDF]

open access: yesPLoS ONE, 2012
BackgroundMembers of the WhiB-like (Wbl) protein family possess iron-sulfur clusters and are implicated in the regulation of developmental processes in Actinomycetes. Mycobacterium tuberculosis possesses seven Wbl proteins.
Laura J Smith   +3 more
doaj   +13 more sources

Revisiting molecular hydrogen signaling in mitochondria: Is the Rieske protein the entry point or a downstream sentinel? [PDF]

open access: yesRedox Biology
A recent study published in Redox Biology (Volume 88, December 2025, 103952) demonstrates that molecular hydrogen (H2) rapidly suppresses mitochondrial Complex III activity through a mechanism involving the Rieske iron-sulfur protein (RISP) and ...
Sergej M. Ostojic
doaj   +2 more sources

Functional Relationships of Two NFU Proteins in Maintaining the Abundances of Mitochondrial Iron–Sulfur Proteins [PDF]

open access: yesPlant Direct
Iron–sulfur clusters are involved in many biological processes, including photosynthetic electron transport in the chloroplast and respiratory electron transport in the mitochondrion. Iron–sulfur cluster biosynthesis requires iron–sulfur carriers such as
Jun Zhao   +7 more
doaj   +2 more sources

Sulfur starvation induces an Fe-replete response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1 [PDF]

open access: yesBMC Microbiology
Background Understanding bacterial responses to nutrient limitation is critical for developing targeted antimicrobial strategies. Sulfur starvation uniquely induces not only genes responsible for sulfur scavenging but also prominent antioxidant defenses.
Chidozie G. Ugochukwu   +4 more
doaj   +2 more sources

The CIA Targeting Complex Is Highly Regulated and Provides Two Distinct Binding Sites for Client Iron-Sulfur Proteins [PDF]

open access: yesCell Reports, 2017
The cytoplasmic iron-sulfur assembly (CIA) targeting complex is required for the transfer of an iron-sulfur (Fe-S) cluster to cytoplasmic and nuclear proteins, but how it engages with client proteins is unknown.
Diana C. Odermatt, Kerstin Gari
doaj   +2 more sources

Anaerobic Expression and Purification of Holo-CCIS, an Artificial Iron-sulfur Protein

open access: yesBio-Protocol, 2021
Iron-sulfur proteins are ubiquitous among all living organisms and are indispensable for almost all metabolic pathways ranging from photosynthesis, respiration, nitrogen, and carbon dioxide cycles.
Bhanu Jagilinki   +3 more
doaj   +1 more source

The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR

open access: yesFrontiers in Molecular Biosciences, 2022
Iron-sulfur proteins play essential roles in a wide variety of cellular processes such as respiration, photosynthesis, nitrogen fixation and magnetoreception.
Tianyang Tong   +25 more
doaj   +1 more source

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