Biological iron-sulfur clusters: Mechanistic insights from mass spectrometry
JC Crack, NE Le Brun - Coordination Chemistry Reviews, 2021 - Elsevier
Iron-sulfur (FeS) clusters are protein cofactors that are ubiquitous in life, performing a wide
range of functions, such as in electron transfer, catalysis and gene regulation. This functional …
range of functions, such as in electron transfer, catalysis and gene regulation. This functional …
Synergy of native mass spectrometry and other biophysical techniques in studies of iron‑sulfur cluster proteins and their assembly
JC Crack, NE Le Brun - Biochimica et Biophysica Acta (BBA)-Molecular …, 2024 - Elsevier
The application of mass spectrometric methodologies has revolutionised biological
chemistry, from identification through to structural and conformational studies of proteins and …
chemistry, from identification through to structural and conformational studies of proteins and …
Sensing mechanisms of iron–sulfur cluster regulatory proteins elucidated using native mass spectrometry
JC Crack, E Gray, NE Le Brun - Dalton Transactions, 2021 - pubs.rsc.org
The ability to sense and respond to various key environmental cues is important for the
survival and adaptability of many bacteria, including pathogens. The particular sensitivity of …
survival and adaptability of many bacteria, including pathogens. The particular sensitivity of …
Native mass spectrometry of iron-sulfur proteins
JC Crack, NE Le Brun - Fe-S proteins: methods and protocols, 2021 - Springer
Iron-sulfur clusters constitute a large and widely distributed group of protein cofactors that
play key roles in a wide range of metabolic processes. The inherent reactivity of iron-sulfur …
play key roles in a wide range of metabolic processes. The inherent reactivity of iron-sulfur …
Mass spectrometric studies of Cu (I)-binding to the N-terminal domains of B. subtilis CopA and influence of bacillithiol
KL Kay, CJ Hamilton, NE Le Brun - Journal of Inorganic Biochemistry, 2019 - Elsevier
CopA is a Cu (I)-exporting transmembrane P 1B-type ATPase from Bacillus subtilis. It
contains two N-terminal cytoplasmic domains, CopAab, which bind Cu (I) with high affinity …
contains two N-terminal cytoplasmic domains, CopAab, which bind Cu (I) with high affinity …
Mechanism of resistance focusing on copper, mercury and arsenic in extremophilic organisms, how acidophiles and thermophiles cope with these metals
J Norambuena - Physiological and Biotechnological Aspects of …, 2020 - Elsevier
Extremophiles usually live in environment that are naturally higher in metal concentrations,
either because they naturally live in acid environments where metal solubility is higher than …
either because they naturally live in acid environments where metal solubility is higher than …