N. L. Le Brun

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A New Role for Heme, Facilitating Release of Iron from the Bacterioferritin Iron Biomineral*

G. Moore, S. Andrews, S. Yasmin, 2010, The Journal of Biological Chemistry.

The dddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide.

J. Todd, N. L. Le Brun, A. Johnston, 2010, Microbiology.

Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD

G. Moore, L. Hederstedt, N. L. Le Brun, 2009, The Journal of Biological Chemistry.

Reaction of O2 with a diiron protein generates a mixed-valent Fe2+/Fe3+ center and peroxide

Rhona K. Stuart, G. Moore, Michael T. Wilson, 2019, Proceedings of the National Academy of Sciences.

Sensing mechanisms of iron–sulfur cluster regulatory proteins elucidated using native mass spectrometry

Jason C. Crack, N. L. Le Brun, E. Gray, 2021, Dalton transactions.

Mass Spectrometric Identification of [4Fe-4S](NO)x Intermediates of Nitric Oxide Sensing by Regulatory Iron-Sulfur Cluster Proteins.

Jason C. Crack, N. L. Le Brun, 2019, Chemistry.

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

M. Buttner, Jason C. Crack, N. L. Le Brun, 2020, The Journal of Biological Chemistry.

Bacterial iron detoxification at the molecular level.

G. Moore, Michael T. Wilson, A. Hemmings, 2020, The Journal of biological chemistry.

Biological iron-sulfur clusters: Mechanistic insights from mass spectrometry

Jason C. Crack, N. L. Le Brun, N. L. Brun, 2021, Coordination Chemistry Reviews.

Electron and proton transfers modulate DNA binding by the transcription regulator RsrR.

A. Volbeda, P. Amara, J. Fontecilla-Camps, 2020, Journal of the American Chemical Society.

Mechanistic insights into the key marine dimethylsulfoniopropionate synthesis enzyme DsyB/DSYB

Xiu-Lan Chen, Jason C. Crack, Yin Chen, 2022, mLife.

nosX is essential for whole-cell N2O reduction in Paracoccus denitrificans but not for assembly of copper centres of nitrous oxide reductase

D. Richardson, N. L. Le Brun, M. J. Torres, 2020, Microbiology.

Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy.

G. Moore, S. Yasmin, N. L. Le Brun, 2009, Biochemistry.

Insights into methionine S-methylation in diverse organisms

J. Banfield, Kang Li, Xiu-Lan Chen, 2022, Nature Communications.

Key carboxylate residues for iron transit through the prokaryotic ferritin SynFtn

A. Hemmings, N. L. Le Brun, J. Bradley, 2021, Microbiology.

Mass spectrometry of B. subtilis CopZ: Cu(i)-binding and interactions with bacillithiol.

N. L. Le Brun, C. Hamilton, Kristine L. Kay, 2016, Metallomics : integrated biometal science.

Protein encapsulation within the internal cavity of a bacterioferritin

G. Moore, N. L. Le Brun, J. Bradley, 2022, Nanoscale.

Interaction of nitric oxide with non-haem iron sites of Escherichia coli bacterioferritin: reduction of nitric oxide to nitrous oxide and oxidation of iron(II) to iron(III).

G. Moore, A. Thomson, S. Andrews, 1997, The Biochemical journal.

Iron-sulfur clusters as biological sensors: the chemistry of reactions with molecular oxygen and nitric oxide.

Jason C. Crack, Jeffrey Green, A. Thomson, 2014, Accounts of chemical research.

Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin.

G. Moore, J. Findlay, A. Thomson, 1994, The Biochemical journal.

The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX

A. Pastore, D. Svergun, P. Konarev, 2018, Front. Mol. Biosci..

Molecular mechanism of the dual regulation of bacterial iron sulfur cluster biogenesis by CyaY and IscX

A. Pastore, D. Svergun, P. Konarev, 2017, bioRxiv.

NosL is a dedicated copper chaperone for assembly of the CuZ center of nitrous oxide reductase† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c9sc01053j

D. Richardson, N. L. Le Brun, J. Bradley, 2019, Chemical science.

Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors

A. Volbeda, J. Fontecilla-Camps, Jason C. Crack, 2022, Communications Biology.

Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein

Jason C. Crack, Jeffrey Green, A. Thomson, 2012, Proceedings of the National Academy of Sciences.

Influence of the environment on the [4Fe-4S]2+ to [2Fe-2S]2+ cluster switch in the transcriptional regulator FNR.

Jason C. Crack, Jeffrey Green, A. Thomson, 2008, Journal of the American Chemical Society.

Detection of Sulfide Release from the Oxygen-sensing [4Fe-4S] Cluster of FNR*

Jason C. Crack, Jeffrey Green, A. Thomson, 2006, Journal of Biological Chemistry.

CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA.

C. Harwood, N. L. Le Brun, J. Cavet, 2003, FEMS microbiology letters.

Diversity of Fe2+ entry and oxidation in ferritins.

G. Moore, N. L. Le Brun, J. Bradley, 2017, Current opinion in chemical biology.

Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin

G. Moore, A. Hemmings, N. L. Le Brun, 2015, Angewandte Chemie.

The Transcriptional Repressor Protein NsrR Senses Nitric Oxide Directly via a [2Fe-2S] Cluster

N. Tucker, R. Dixon, G. Chandra, 2008, PloS one.

Mycobacterium tuberculosis WhiB1 is an essential DNA-binding protein with a nitric oxide-sensitive iron-sulfur cluster.

Jason C. Crack, Jeffrey Green, A. Thomson, 2010, The Biochemical journal.

NsrR from Streptomyces coelicolor Is a Nitric Oxide-sensing [4Fe-4S] Cluster Protein with a Specialized Regulatory Function*

Jason C. Crack, A. Thomson, S. Kamali, 2015, The Journal of Biological Chemistry.

Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily

Jason C. Crack, M. Hutchings, N. L. Le Brun, 2016, Scientific Reports.

Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA

Jason C. Crack, J. Todd, N. L. Le Brun, 2019, eLife.

Protein-template-driven formation of polynuclear iron species.

C. Cooper, G. Moore, Michael T. Wilson, 2004, Journal of the American Chemical Society.

Formation of protein-coated iron minerals.

G. Moore, N. L. Le Brun, A. Lewin, 2005, Dalton transactions.

Copper-mediated dimerization of CopZ, a predicted copper chaperone from Bacillus subtilis.

A. Leech, N. L. Le Brun, Margaret A. Kihlken, 2002, The Biochemical journal.

Purification and Characterization of the Isoprene Monooxygenase from Rhodococcus sp. Strain AD45

J. Murrell, A. Crombie, N. L. Le Brun, 2022, Applied and environmental microbiology.

Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD.

M. Buttner, Jason C. Crack, A. Thomson, 2009, Biochemistry.

Redox-Sensing Iron-Sulfur Cluster Regulators.

Jason C. Crack, N. L. Le Brun, 2017, Antioxidants & redox signaling.

MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.

G. Moore, A. Thomson, N. L. Le Brun, 1995, Biochimica et Biophysica Acta.

Identification of the ferroxidase centre of Escherichia coli bacterioferritin.

P. Harrison, G. Moore, A. Thomson, 1995, The Biochemical journal.

Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre.

G. Moore, N. L. Le Brun, J. Bradley, 2017, Metallomics : integrated biometal science.

Ferritins: furnishing proteins with iron

G. Moore, N. L. Le Brun, J. Bradley, 2016, JBIC Journal of Biological Inorganic Chemistry.

The B-type Channel Is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin*

M. Murphy, G. Moore, A. Mauk, 2014, The Journal of Biological Chemistry.

Iron core mineralisation in prokaryotic ferritins.

M. Murphy, G. Moore, A. Mauk, 2010, Biochimica et biophysica acta.

Structural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core Formation*

G. Moore, A. Mauk, N. L. Le Brun, 2009, The Journal of Biological Chemistry.

Structural basis for iron mineralization by bacterioferritin.

G. Moore, N. L. Le Brun, A. Crow, 2009, Journal of the American Chemical Society.

Effect of phosphate on bacterioferritin-catalysed iron(II) oxidation

G. Moore, C. Singleton, N. L. Le Brun, 2004, JBIC Journal of Biological Inorganic Chemistry.

Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites.

G. Moore, M. R. Mauk, A. Mauk, 1996, FEBS letters.

Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center.

G. Moore, N. L. Le Brun, A. Lewin, 2003, Biochemistry.

Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin

G. Moore, Michael T. Wilson, A. Thomson, 1993, FEBS letters.

The O2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion

P. Artymiuk, A. Jervis, Jason C. Crack, 2009, Proceedings of the National Academy of Sciences.

Superoxide-mediated amplification of the oxygen-induced switch from [4Fe-4S] to [2Fe-2S] clusters in the transcriptional regulator FNR

Jason C. Crack, Jeffrey Green, A. Thomson, 2007, Proceedings of the National Academy of Sciences.

PerR controls oxidative stress defence and aerotolerance but not motility-associated phenotypes of Campylobacter jejuni.

L. Clissold, A. H. V. van Vliet, F. Mulholland, 2015, Microbiology.

The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu(I) ions.

C. Singleton, N. L. Le Brun, 2009, Dalton transactions.

Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA.

L. Tenori, R. Boetzel, L. Banci, 2008, The Biochemical journal.

An EPR investigation of non‐haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate

G. Moore, A. Thomson, J. Guest, 1993, FEBS letters.

Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation.

L. Tenori, C. Singleton, N. L. Le Brun, 2017, Chemical communications.

Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA.

S. Hearnshaw, A. Hemmings, C. Singleton, 2009, The Biochemical journal.

High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ.

C. Singleton, N. L. Le Brun, Liang Zhou, 2008, The Biochemical journal.

Structure of a Wbl protein and implications for NO sensing by M. tuberculosis

A. Hounslow, M. Williamson, Jason C. Crack, 2017, Nature Communications.

RsmA Is an Anti-sigma Factor That Modulates Its Activity through a [2Fe-2S] Cluster Cofactor*

Jason C. Crack, M. Hutchings, N. L. Le Brun, 2007, Journal of Biological Chemistry.

Genes required for cytochrome c synthesis inBacillus subtilis

L. Hederstedt, N. L. Le Brun, J. Bengtsson, 2000, Molecular microbiology.

Iron–sulfur clusters as inhibitors and catalysts of viral replication

F. Armstrong, W. Hagen, P. Hagedoorn, 2022, Nature Chemistry.

Fe-haem bound to Escherichia coli bacterioferritin accelerates iron core formation by an electron transfer mechanism.

G. Moore, A. Mauk, N. L. Le Brun, 2012, The Biochemical journal.

Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies.

P. Harrison, G. Moore, A. Thomson, 1993, The Biochemical journal.

Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H2O2 but Slowly with O2

G. Moore, Michael T. Wilson, J. Worrall, 2021, Angewandte Chemie.

Iron Detoxification Properties of Escherichia coliBacterioferritin

G. Moore, N. L. Le Brun, F. Bou-Abdallah, 2002, The Journal of Biological Chemistry.

The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin.

G. Moore, A. Thomson, N. L. Le Brun, 2000, Biochemistry.

Mechanism of Ferrous Iron Binding and Oxidation by Ferritin from a Pennate Diatom*

N. L. Le Brun, Michael E. P. Murphy, Raz Abdulqadir, 2013, The Journal of Biological Chemistry.

Iron Detoxification Properties of Escherichia coliBacterioferritin

G. Moore, N. L. Le Brun, N. Chasteen, 2002, The Journal of Biological Chemistry.

Mechanisms of iron mineralization in ferritins: one size does not fit all

G. Moore, N. L. Le Brun, J. Bradley, 2014, JBIC Journal of Biological Inorganic Chemistry.

Differentiated, Promoter-specific Response of [4Fe-4S] NsrR DNA Binding to Reaction with Nitric Oxide*

Jason C. Crack, A. Thomson, M. Hutchings, 2016, The Journal of Biological Chemistry.

Mechanistic Insight into the Nitrosylation of the [4Fe−4S] Cluster of WhiB-like Proteins

M. Buttner, Jason C. Crack, Jeffrey Green, 2010, Journal of the American Chemical Society.

Signal perception by FNR: the role of the iron-sulfur cluster.

A. Jervis, Jason C. Crack, Jeffrey Green, 2008, Biochemical Society transactions.

Reactions of nitric oxide and oxygen with the regulator of fumarate and nitrate reduction, a global transcriptional regulator, during anaerobic growth of Escherichia coli.

A. Jervis, Jason C. Crack, Jeffrey Green, 2008, Methods in enzymology.

Crystal Structure of the Transcription Regulator RsrR Reveals a [2Fe-2S] Cluster Coordinated by Cys, Glu, and His Residues.

A. Volbeda, P. Amara, J. Fontecilla-Camps, 2019, Journal of the American Chemical Society.

There's NO stopping NsrR, a global regulator of the bacterial NO stress response.

N. Tucker, R. Dixon, M. Hutchings, 2010, Trends in microbiology.

Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit.

J. Yu, N. L. Le Brun, N. Brun, 1998, The Journal of biological chemistry.

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA*

N. L. Le Brun, Allister Crow, Richard M Acheson, 2004, Journal of Biological Chemistry.

Bacillus subtilis ResA Is a Thiol-Disulfide Oxidoreductase involved in Cytochrome c Synthesis*

L. Hederstedt, N. L. Le Brun, L. Erlendsson, 2003, The Journal of Biological Chemistry.

The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress

Jason C. Crack, Jeffrey Green, J. Cole, 2022, Journal of the American Chemical Society.

Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria† †Electronic supplementary information (ESI) available: Details of M. marinum CYPome, experimental methods and additional data tables and figures. See DOI: 10.1039/c8sc01286e

S. Bell, T. Pukala, N. L. Le Brun, 2018, Chemical science.

Bacterial iron-sulfur regulatory proteins as biological sensor-switches.

Jason C. Crack, Jeffrey Green, A. Thomson, 2012, Antioxidants & redox signaling.

CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(I)-binding properties of CopAab.

C. Singleton, N. L. Le Brun, Liang Zhou, 2012, Dalton transactions.

Cu(I)‐ and proton‐binding properties of the first N‐terminal soluble domain of Bacillus subtilis CopA

G. Moore, C. Singleton, N. L. Le Brun, 2012, The FEBS journal.

Structure and Functional Properties of Bacillus subtilis Endospore Biogenesis Factor StoA

L. Hederstedt, N. L. Le Brun, Yiming Liu, 2009, Journal of Biological Chemistry.

The Active-Site Cysteinyls and Hydrophobic Cavity Residues of ResA Are Important for Cytochrome c Maturation in Bacillus subtilis

L. Hederstedt, N. L. Le Brun, Christopher T C Hodson, 2008, Journal of bacteriology.

Second Coordination Sphere Effects on the Mechanistic Pathways for Dioxygen Activation by a Ferritin: Involvement of a Tyr Radical and the Identification of a Cation Binding Site

S. D. de Visser, N. L. Le Brun, J. Bradley, 2022, Chembiochem : a European journal of chemical biology.

Heme-responsive DNA Binding by the Global Iron Regulator Irr from Rhizobium leguminosarum*

C. Singleton, G. White, J. Todd, 2010, The Journal of Biological Chemistry.

Native Mass Spectrometry of Iron-Sulfur Proteins.

Jason C. Crack, N. L. Le Brun, 2021, Methods in molecular biology.

Iron-sulfur cluster sensor-regulators.

Jason C. Crack, Jeffrey Green, A. Thomson, 2012, Current opinion in chemical biology.

Mechanism of [4Fe-4S](Cys)4 Cluster Nitrosylation Is Conserved among NO-responsive Regulators*

Jason C. Crack, Jeffrey Green, A. Thomson, 2013, The Journal of Biological Chemistry.

Mass spectrometric identification of intermediates in the O2-driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR

Jason C. Crack, A. Thomson, N. L. Le Brun, 2017, Proceedings of the National Academy of Sciences.

Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations

H. Stark, W. Hagen, M. Piccioli, 2022, Frontiers in Molecular Biosciences.

Structure of a Wbl protein and implications for NO sensing by M. tuberculosis

A. Hounslow, M. Williamson, Jason C. Crack, 2017, Nature Communications.

Three Pseudomonas putida FNR Family Proteins with Different Sensitivities to O2*

Jason C. Crack, Jeffrey Green, A. Thomson, 2015, The Journal of Biological Chemistry.

Cmr is a redox-responsive regulator of DosR that contributes to M. tuberculosis virulence

J. Saldanha, I. Nobeli, V. Makarov, 2017, Nucleic acids research.

A Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage*

M. Murphy, G. Moore, N. L. Le Brun, 2015, The Journal of Biological Chemistry.

Andrew James Thomson. 31 July 1940 — 2 March 2021

F. Armstrong, Michael T. Wilson, N. L. Le Brun, 2022, BIOGRAPHICAL MEMOIRS OF FELLOWS OF THE ROYAL SOCIETY.

Influence of association state and DNA binding on the O2-reactivity of [4Fe-4S] fumarate and nitrate reduction (FNR) regulator

Jason C. Crack, Jeffrey Green, A. Thomson, 2014, The Biochemical journal.

The role of ResA in type II cytochrome c maturation.

N. L. Le Brun, A. Oubrie, A. Crow, 2005, Biochemical Society transactions.

Heme binding to the second, lower‐affinity site of the global iron regulator Irr from Rhizobium leguminosarum promotes oligomerization

C. Singleton, G. White, J. Todd, 2011, The FEBS journal.

Techniques for the production, isolation, and analysis of iron-sulfur proteins.

Jason C. Crack, Jeffrey Green, A. Thomson, 2014, Methods in molecular biology.

Generation of 34S-substituted protein-bound [4Fe-4S] clusters using 34S-L-cysteine

Jason C. Crack, N. L. Le Brun, Melissa Y. Y. Stewart, 2019, Biology methods & protocols.

Mass spectrometric detection of iron nitrosyls, sulfide oxidation and mycothiolation during nitrosylation of the NO sensor [4Fe–4S] NsrR† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8cc01339j

Jason C. Crack, N. L. Le Brun, C. Hamilton, 2018, Chemical communications.

Crystal structures of the NO sensor NsrR reveal how its iron-sulfur cluster modulates DNA binding

A. Volbeda, J. Fontecilla-Camps, Jason C. Crack, 2017, Nature Communications.

Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA.

L. Hederstedt, N. L. Le Brun, Lars Hederstedt, 2008, The Biochemical journal.

Ferritins: furnishing proteins with iron

G. Moore, N. L. Le Brun, J. Bradley, 2016, JBIC Journal of Biological Inorganic Chemistry.

NosL is a dedicated copper chaperone for assembly of the CuZ center of nitrous oxide reductase† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c9sc01053j

D. Richardson, N. L. Le Brun, J. Bradley, 2019, Chemical science.

Molecular Basis for Specificity of the Extracytoplasmic Thioredoxin ResA*

N. L. Le Brun, A. Oubrie, A. Crow, 2006, Journal of Biological Chemistry.

PerR controls oxidative stress defence and aerotolerance but not motility-associated phenotypes of Campylobacter jejuni.

L. Clissold, A. H. V. van Vliet, F. Mulholland, 2015, Microbiology.

Mechanism of [4Fe-4S](Cys)4 Cluster Nitrosylation Is Conserved among NO-responsive Regulators*

Jason C. Crack, Jeffrey Green, A. Thomson, 2013, The Journal of Biological Chemistry.

Mechanistic Insight into the Nitrosylation of the [4Fe−4S] Cluster of WhiB-like Proteins

M. Buttner, Jason C. Crack, Jeffrey Green, 2010, Journal of the American Chemical Society.

Jason C. Crack, N. L. Le Brun, C. Hamilton, 2018, Chemical communications.

Biochemical properties of Paracoccus denitrificans FnrP: reactions with molecular oxygen and nitric oxide

Jason C. Crack, A. Thomson, M. Hutchings, 2016, JBIC Journal of Biological Inorganic Chemistry.

From cultivation to cancer: formation of N-nitrosamines and other carcinogens in smokeless tobacco and their mutagenic implications

A. Joerger, B. Blount, Jason C. Crack, 2023, Critical reviews in toxicology.

There's NO stopping NsrR, a global regulator of the bacterial NO stress response.

N. Tucker, R. Dixon, M. Hutchings, 2010, Trends in microbiology.

Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron–sulfur cluster assembly

A. Pastore, Jason C. Crack, N. L. Le Brun, 2022, Chemical Science.

NBP35 interacts with DRE2 in the maturation of cytosolic iron‐sulphur proteins in Arabidopsis thaliana

J. Balk, Jason C. Crack, K. Bych, 2017, The Plant journal : for cell and molecular biology.

Replacement of methionine as the axial ligand of Achromobacter cycloclastes cytochrome c554 at high pH values revealed by absorption, EPR and MCD spectroscopy.

A. Thomson, M. Y. Liu, W. Payne, 1994, Biochemical and biophysical research communications.

The N-terminal domains of Bacillus subtilis CopA do not form a stable complex in the absence of their inter-domain linker.

G. Moore, N. L. Le Brun, Kristine L. Kay, 2018, Biochimica et biophysica acta. Proteins and proteomics.