The [4Fe‐4S]‐Cluster of HydF is not Required for the Binding and Transfer of the Diiron Site of [FeFe]‐Hydrogenases
Sign Up to like & getrecommendations! Published in 2023 at "ChemBioChem"
DOI: 10.1002/cbic.202300222
Abstract: The active site of [FeFe]‐hydrogenases contains a cubane [4Fe‐4S]‐cluster and a unique diiron cluster with biologically unusual CO and CN− ligands. The biogenesis of this diiron site, termed [2FeH], requires the maturation proteins HydE, HydF… read more here.
Keywords: transfer; hydf; site; cluster ... See more keywords
A conserved motif liganding the [4Fe–4S] cluster in [4Fe–4S] fumarases prevents irreversible inactivation of the enzyme during hydrogen peroxide stress
Sign Up to like & getrecommendations! Published in 2019 at "Redox Biology"
DOI: 10.1016/j.redox.2019.101296
Abstract: Organisms have evolved two different classes of the ubiquitous enzyme fumarase: the [4Fe–4S] cluster-containing class I enzymes are oxidant-sensitive, whereas the class II enzymes are iron-free and therefore oxidant-resistant. When hydrogen peroxide (H2O2) attacks the… read more here.
Keywords: 4fe fumarases; hydrogen peroxide; fumarase; 4fe cluster ... See more keywords
Modification of the 4Fe-4S Cluster Charge Transport Pathway Alters RNA Synthesis by Yeast DNA Primase.
Sign Up to like & getrecommendations! Published in 2022 at "Biochemistry"
DOI: 10.1021/acs.biochem.2c00100
Abstract: DNA synthesis during replication begins with the generation of an ∼10-nucleotide primer by DNA primase. Primase contains a redox-active 4Fe-4S cluster in the C-terminal domain of the p58 subunit (p58C). The redox state of this… read more here.
Keywords: 4fe cluster; primase; dna; charge transport ... See more keywords
Characterization of the Geometrical and Electronic Structures of the Active Site and Its Effects on the Surrounding Environment in Reduced High-Potential Iron-Sulfur Proteins Investigated by the Density Functional Theory Approach.
Sign Up to like & getrecommendations! Published in 2023 at "Inorganic chemistry"
DOI: 10.1021/acs.inorgchem.2c03617
Abstract: The high-potential iron-sulfur protein (HiPIP) is an electron-transporting protein that functions in the photosynthetic electron-transfer system and possesses a cubane-type [4Fe-4S] cluster in the active center. Characterization of the geometrical and electronic structures of the… read more here.
Keywords: electronic structures; geometrical electronic; environment; iron ... See more keywords
Protein-Interaction Affinity Gradient Drives [4Fe–4S] Cluster Insertion in Human Lipoyl Synthase
Sign Up to like & getrecommendations! Published in 2022 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.1c13626
Abstract: Human lipoyl synthase (LIAS) is an enzyme containing two [4Fe–4S] clusters (named FeSRS and FeSaux) involved in the biosynthesis of the lipoyl cofactor. The mechanism by which a [4Fe–4S] cluster is inserted into LIAS has… read more here.
Keywords: lipoyl synthase; protein interaction; human lipoyl; cluster ... See more keywords
Substrate-Dependent Conformational Switch of the Noncubane [4Fe-4S] Cluster in Heterodisulfide Reductase HdrB.
Sign Up to like & getrecommendations! Published in 2022 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.2c10885
Abstract: The noncubane [4Fe-4S] cluster identified in the active site of heterodisulfide reductase (HdrB) displays a unique geometry among Fe-S cofactors found in metalloproteins. Here we employ resonance Raman (RR) spectroscopy and density functional theory (DFT)… read more here.
Keywords: noncubane 4fe; reductase hdrb; cluster; 4fe cluster ... See more keywords
A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of Clostridium acetobutylicum [FeFe]-hydrogenase I
Sign Up to like & getrecommendations! Published in 2022 at "Chemical Science"
DOI: 10.1039/d1sc07120c
Abstract: One of the many functions of reduction–oxidation (redox) cofactors is to mediate electron transfer in biological enzymes catalyzing redox-based chemical transformation reactions. There are numerous examples of enzymes that utilize redox cofactors to form electron… read more here.
Keywords: electron transfer; 4fe cluster; reactivity; transfer ... See more keywords
A subclass of archaeal U8-tRNA sulfurases requires a [4Fe–4S] cluster for catalysis
Sign Up to like & getrecommendations! Published in 2022 at "Nucleic Acids Research"
DOI: 10.1093/nar/gkac1156
Abstract: Abstract Sulfuration of uridine 8, in bacterial and archaeal tRNAs, is catalyzed by enzymes formerly known as ThiI, but renamed here TtuI. Two different classes of TtuI proteins, which possess a PP-loop-containing pyrophosphatase domain that… read more here.
Keywords: catalysis; cluster; subclass archaeal; 4fe cluster ... See more keywords
SufR, a [4Fe-4S] Cluster-Containing Transcription Factor, Represses the sufRBDCSU Operon in Streptomyces avermitilis Iron-Sulfur Cluster Assembly
Sign Up to like & getrecommendations! Published in 2020 at "Applied and Environmental Microbiology"
DOI: 10.1128/aem.01523-20
Abstract: Fe–S clusters function as cofactors of proteins controlling diverse biological processes, such as respiration, photosynthesis, nitrogen fixation, DNA replication, and gene regulation. The mechanism of how Actinobacteria regulate the expression of the sole Fe-S cluster… read more here.
Keywords: system; cluster; cluster assembly; operon ... See more keywords
The Arabidopsis Mitochondrial Glutaredoxin GRXS15 Provides [2Fe-2S] Clusters for ISCA-Mediated [4Fe-4S] Cluster Maturation
Sign Up to like & getrecommendations! Published in 2020 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms21239237
Abstract: Iron-sulfur (Fe-S) proteins are crucial for many cellular functions, particularly those involving electron transfer and metabolic reactions. An essential monothiol glutaredoxin GRXS15 plays a key role in the maturation of plant mitochondrial Fe-S proteins. However,… read more here.
Keywords: spectroscopy; 4fe cluster; isca1a; cluster ... See more keywords
Disentangling Unusual Catalytic Properties and the Role of the [4Fe-4S] Cluster of Three Endonuclease III from the Extremophile D. radiodurans
Sign Up to like & getrecommendations! Published in 2022 at "Molecules"
DOI: 10.3390/molecules27134270
Abstract: Endonuclease III (EndoIII) is a bifunctional DNA glycosylase with specificity for a broad range of oxidized DNA lesions. The genome of an extremely radiation- and desiccation-resistant bacterium, Deinococcus radiodurans, possesses three genes encoding for EndoIII-like… read more here.
Keywords: endonuclease iii; role; cluster; activity ... See more keywords