Jason C. Crack
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View article: Yeast [FeFe]-hydrogenase-like protein Nar1 binds a [2Fe–2S] cluster
Yeast [FeFe]-hydrogenase-like protein Nar1 binds a [2Fe–2S] cluster Open
Nar1 is an essential iron–sulphur protein biogenesis component in eukaryotes that can bind not only two [4Fe–4S] clusters but also a newly identified [2Fe–2S] cluster.
View article: Cluster occupancy- and oxidation state-dependence of Yersinia enterocolitica IscR DNA binding
Cluster occupancy- and oxidation state-dependence of Yersinia enterocolitica IscR DNA binding Open
View article: ArnR binds a [4Fe–4S] cluster and indirectly senses anaerobicity in <i>Corynebacteria</i>
ArnR binds a [4Fe–4S] cluster and indirectly senses anaerobicity in <i>Corynebacteria</i> Open
Corynebacteria are commercially and medically important Gram-positive bacteria that can switch from aerobic to anaerobic respiration in response to low O2 and the availability of nitrate as an alternative electron acceptor. The narKGHJI op…
View article: Yeast [FeFe]-hydrogenase-like protein Nar1 can bind not only two [4Fe-4S] clusters but also a [2Fe-2S] cluster
Yeast [FeFe]-hydrogenase-like protein Nar1 can bind not only two [4Fe-4S] clusters but also a [2Fe-2S] cluster Open
Nar1 is an essential eukaryotic protein proposed to function as an iron-sulfur (Fe/S) cluster trafficking factor in the cytosolic iron-sulfur assembly (CIA) machinery. However, such a role has remained unclear due to difficulties in purify…
View article: Synergy of native mass spectrometry and other biophysical techniques in studies of iron‑sulfur cluster proteins and their assembly
Synergy of native mass spectrometry and other biophysical techniques in studies of iron‑sulfur cluster proteins and their assembly Open
The application of mass spectrometric methodologies has revolutionised biological chemistry, from identification through to structural and conformational studies of proteins and other macromolecules. Native mass spectrometry (MS), in which…
View article: Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway
Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway Open
All sulfur transfer pathways generally have in common an l -cysteine desulfurase as the initial sulfur-mobilizing enzyme, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell. In Escher…
View article: CyaY and TusA regulate ISC- and SUF-mediated <scp>l</scp>-cysteine desulfurase activity
CyaY and TusA regulate ISC- and SUF-mediated <span>l</span>-cysteine desulfurase activity Open
CyaY, the frataxin homolog of Escherichia coli , is known to regulate ISC iron–sulfur cluster assembly through binding to IscS. It also interacts with the SUF system, through binding to, and attenuating activity of, SufS.
View article: Binding of a single nitric oxide molecule is sufficient to disrupt DNA binding of the nitrosative stress regulator NsrR
Binding of a single nitric oxide molecule is sufficient to disrupt DNA binding of the nitrosative stress regulator NsrR Open
The mechanism of NO sensing by the nitrosative stress regulator NsrR is elucidated. Binding of a single NO to one of the [4Fe–4S] clusters of dimeric NsrR results in dissociation of its complex with DNA.
View article: From cultivation to cancer: formation of <i>N</i> -nitrosamines and other carcinogens in smokeless tobacco and their mutagenic implications
From cultivation to cancer: formation of <i>N</i> -nitrosamines and other carcinogens in smokeless tobacco and their mutagenic implications Open
Tobacco use is a major cause of preventable morbidity and mortality globally. Tobacco products, including smokeless tobacco (ST), generally contain tobacco-specific N-nitrosamines (TSNAs), such as N'-nitrosonornicotine (NNN) …
View article: Probing the Reactivity of [4Fe-4S] Fumarate and Nitrate Reduction (FNR) Regulator with O2 and NO: Increased O2 Resistance and Relative Specificity for NO of the [4Fe-4S] L28H FNR Cluster
Probing the Reactivity of [4Fe-4S] Fumarate and Nitrate Reduction (FNR) Regulator with O2 and NO: Increased O2 Resistance and Relative Specificity for NO of the [4Fe-4S] L28H FNR Cluster Open
The Escherichia coli fumarate and nitrate reduction (FNR) regulator acts as the cell’s master switch for the transition between anaerobic and aerobic respiration, controlling the expression of >300 genes in response to O2 availability. Oxy…
View article: Liquid-chromatography mass spectrometry describes post-translational modification of Shewanella outer membrane proteins
Liquid-chromatography mass spectrometry describes post-translational modification of Shewanella outer membrane proteins Open
Electrogenic bacteria deliver excess respiratory electrons to externally located metal oxide particles and electrodes. The biochemical basis for this process is arguably best understood for species of Shewanella where the integral membrane…
View article: Site-specific encoding of photoactivity and photoreactivity into antibody fragments
Site-specific encoding of photoactivity and photoreactivity into antibody fragments Open
View article: Liquid-Chromatography Mass Spectrometry Describes Post-Translational Modification of <i>Shewanella</i> Outer Membrane Proteins
Liquid-Chromatography Mass Spectrometry Describes Post-Translational Modification of <i>Shewanella</i> Outer Membrane Proteins Open
LC-MS data for MtrCAB complexes from Shewanella oneidensis MR-1 and Shewanella baltica OS-185.LC-MS data for a soluble form of MtrC from Shewanella oneidensis MR-1 carrying a C-terminal Strep II tag.
View article: Stabilisation of the RirA [4Fe–4S] cluster results in loss of iron-sensing function
Stabilisation of the RirA [4Fe–4S] cluster results in loss of iron-sensing function Open
The regulator RirA senses Fe through its [4Fe–4S] cluster, which may have only three Cys ligands from the protein. Addition of a likely fourth Asp ligand stabilised the cluster, rendering it unable to sense Fe and locked into its DNA-bindi…
View article: Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron–sulfur cluster assembly
Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron–sulfur cluster assembly Open
Time-resolved native mass spectrometry was used to investigate iron–sulfur cluster assembly on IscU. Data revealed a concerted assembly process in which sulfur (S 0 ) transfer must occur first if IscU is in its Zn 2+ -bound form.
View article: Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis
Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis Open
Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of inorganic sulfur. The active sites of these enzymes contain low-spin c-type heme with Cys-/His axial ligation. However, the reduction potentials of th…
View article: Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors
Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors Open
Several transcription factors of the Rrf2 family use an iron-sulfur cluster to regulate DNA binding through effectors such as nitric oxide (NO), cellular redox status and iron levels. [4Fe-4S]-NsrR from Streptomyces coelicolor ( Sc NsrR) m…
View article: Mechanistic insights into the key marine dimethylsulfoniopropionate synthesis enzyme DsyB/DSYB
Mechanistic insights into the key marine dimethylsulfoniopropionate synthesis enzyme DsyB/DSYB Open
Marine algae and bacteria produce approximately eight billion tonnes of the organosulfur molecule dimethylsulfoniopropionate (DMSP) in Earth's surface oceans annually. DMSP is an antistress compound and, once released into the environment,…
View article: The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress
The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress Open
Previously characterized nitrite reductases fall into three classes: siroheme-containing enzymes (NirBD), cytochrome c hemoproteins (NrfA and NirS), and copper-containing enzymes (NirK). We show here that the di-iron protein YtfE re…
View article: Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insight into the Mechanism of Oxidative Catalysis
Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insight into the Mechanism of Oxidative Catalysis Open
Data from Mass Spectrometry, Electronic Absorbance Spectroscopy, Magnetic Circular Dichroism (MCD) Spectroscopy and Protein Film Electrochemistry (PFE) in studies of the reaction between sulfite and the diheme thiosulfate dehydrogenase fro…
View article: Mechanistic insight into DsyB/DSYB, key enzymes in marine dimethylsulfoniopropionate synthesis
Mechanistic insight into DsyB/DSYB, key enzymes in marine dimethylsulfoniopropionate synthesis Open
Marine algae and bacteria produce eight billion tonnes of the organosulfur molecule dimethylsulfoniopropionate (DMSP) in Earth’s surface oceans every year. DMSP is an anti-stress compound and, once released into the environment, a major nu…
View article: Sensing mechanisms of iron–sulfur cluster regulatory proteins elucidated using native mass spectrometry
Sensing mechanisms of iron–sulfur cluster regulatory proteins elucidated using native mass spectrometry Open
Native mass spectrometry provides novel insight into protein cofactor (e.g. iron–sulfur cluster) chemistry.
View article: Author Index
Author Index Open
View article: Interaction of the Streptomyces Wbl protein WhiD with the principal sigma factor σHrdB depends on the WhiD [4Fe-4S] cluster
Interaction of the Streptomyces Wbl protein WhiD with the principal sigma factor σHrdB depends on the WhiD [4Fe-4S] cluster Open
View article: Electron and Proton Transfers Modulate DNA Binding by the Transcription Regulator RsrR
Electron and Proton Transfers Modulate DNA Binding by the Transcription Regulator RsrR Open
The [Fe2S2]-RsrR gene transcription regulator senses the redox status in bacteria by modulating DNA binding, while its cluster cycles between +1 and +2 states-only the latter binds DNA. We have previously shown that R…
View article: Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA
Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA Open
RirA is a global regulator of iron homeostasis in Rhizobium and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or a…
View article: Author response: Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA
Author response: Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA Open
Article Figures and data Abstract eLife digest Introduction Results and discussion Materials and methods Data availability References Decision letter Author response Article and author information Metrics Abstract RirA is a global regulato…
View article: Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe–2S] Cluster Coordinated by Cys, Glu, and His Residues
Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe–2S] Cluster Coordinated by Cys, Glu, and His Residues Open
The recently discovered Rrf2 family transcriptional regulator RsrR coordinates a [2Fe-2S] cluster. Remarkably, binding of the protein to RsrR-regulated promoter DNA sequences is switched on and off through the facile cycling of the [2Fe-2S…
View article: Mass Spectrometric Identification of [4Fe–4S](NO)<sub><i>x</i></sub> Intermediates of Nitric Oxide Sensing by Regulatory Iron–Sulfur Cluster Proteins
Mass Spectrometric Identification of [4Fe–4S](NO)<sub><i>x</i></sub> Intermediates of Nitric Oxide Sensing by Regulatory Iron–Sulfur Cluster Proteins Open
Nitric oxide (NO) can function as both a cytotoxin and a signalling molecule. In both cases, reaction with iron–sulfur (Fe–S) cluster proteins plays an important role because Fe–S clusters are reactive towards NO and so are a primary site …
View article: Generation of 34S-substituted protein-bound [4Fe-4S] clusters using 34S-L-cysteine
Generation of 34S-substituted protein-bound [4Fe-4S] clusters using 34S-L-cysteine Open
The ability to specifically label the sulphide ions of protein-bound iron–sulphur (FeS) clusters with 34S isotope greatly facilitates structure–function studies. In particular, it provides insight when using either spectroscopic techniques…