Results 51 to 60 of about 112,766 (248)

Interaction of the Streptomyces Wbl protein WhiD with the principal sigma factor σHrdB depends on the WhiD [4Fe-4S] cluster [PDF]

open access: yes, 2020
The bacterial protein WhiD belongs to the Wbl family of iron–sulfur [Fe-S] proteins present only in the actinomycetes. In Streptomyces coelicolor, it is required for the late stages of sporulation, but precisely how it functions is unknown.
Bush, Matthew   +4 more
core   +1 more source

Transcriptomic and proteomic analyses of Desulfovibrio vulgaris biofilms: carbon and energy flow contribute to the distinct biofilm growth state. [PDF]

open access: yes, 2012
BackgroundDesulfovibrio vulgaris Hildenborough is a sulfate-reducing bacterium (SRB) that is intensively studied in the context of metal corrosion and heavy-metal bioremediation, and SRB populations are commonly observed in pipe and subsurface ...
Arkin, Adam P   +8 more
core   +3 more sources

Investigating Iron-Sulfur Proteins in Infectious Diseases: A Review of Characterization Techniques

open access: yesInorganics
Iron-sulfur [Fe-S] clusters, comprising coordinated iron and sulfur atoms arranged in diverse configurations, play a pivotal role in redox reactions and various biological processes.
Md Kausar Raza   +2 more
doaj   +1 more source

Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

open access: yesNature Communications, 2021
The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic β- and γ-Proteobacteria.
Tomoaki Kawakami   +6 more
doaj   +1 more source

The site of synthesis of the iron-sulfur subunits of the flavoprotein and iron-protein fractions of human NADH dehydrogenase [PDF]

open access: yes, 1988
The site of synthesis of the iron-sulfur subunits of the flavoprotein and iron-protein fractions of the human respiratory chain NADH dehydrogenase has been investigated to test the possibility that any of them is synthesized in mitochondria.
Attardi, Giuseppe   +4 more
core  

How innate immunity proteins kill bacteria and why they are not prone to resistance [PDF]

open access: yes, 2017
Recent advances on antibacterial activity of peptidoglycan recognition proteins (PGRPs) offer some insight into how innate immunity has retained its antimicrobial effectiveness for millions of years with no frequent emergence of resistant strains. First,
Dziarski, Roman, Gupta, Dipika
core   +1 more source

The diversity and applications of microbial iron metabolism and iron-containing proteins

open access: yesCommunications Biology
This collection reflects research that will advance the understanding of hemoproteins, iron-sulfur cluster proteins and other iron-containing proteins, proteins involved in homeostasis of iron/heme and their regulation, or ecological impacts of iron/heme
Haichun Gao, Ingrid Span
doaj   +1 more source

Primary and secondary oxidative stress in Bacillus [PDF]

open access: yes, 2011
Coping with oxidative stress originating from oxidizing compounds or reactive oxygen species (ROS), associated with the exposure to agents that cause environmental stresses, is one of the prerequisites for an aerobic lifestyle of Bacillus spp. such as B.
Abee, T., Mols, J.M.
core   +3 more sources

Constraint-based modeling of yeast mitochondria reveals the dynamics of protein import and iron-sulfur cluster biogenesis

open access: yesiScience, 2021
Summary: Mitochondria are a hallmark of eukaryal cells and play an important role in cellular metabolism. There is a vast amount of knowledge available on mitochondrial metabolism and essential mitochondrial functions, such as protein import and iron ...
Carl Malina   +3 more
doaj   +1 more source

Iron–sulfur-protein biogenesis in eukaryotes

open access: yesTrends in Biochemical Sciences, 2005
Iron-sulfur (Fe-S) clusters (ISCs) are versatile, ancient co-factors of proteins that are involved in electron transport, enzyme catalysis and regulation of gene expression. The synthesis of ISCs and their insertion into apoproteins involves the function of complex cellular machineries.
Lill, Roland, Mühlenhoff, Ulrich
openaire   +2 more sources

Home - About - Disclaimer - Privacy