Outputs (30)

One His, two His…the emerging roles of histidine in cellular nickel trafficking (2024)
Journal Article
Chivers, P. T., Basak, P., & Maroney, M. J. (2024). One His, two His…the emerging roles of histidine in cellular nickel trafficking. Journal of Inorganic Biochemistry, 259, Article 112668. https://doi.org/10.1016/j.jinorgbio.2024.112668

Biological environments present a complex array of metal-binding ligands. Metal-binding proteins have been the overwhelming focus of study because of their important and well-defined biological roles. Consequently, the presence of functional low mole... Read More about One His, two His…the emerging roles of histidine in cellular nickel trafficking.

Reduction-cleavable desferrioxamine B pulldown system enriches Ni( ii )-superoxide dismutase from a Streptomyces proteome (2023)
Journal Article
Ni, J., Wood, J. L., White, M. Y., Lihi, N., Markham, T. E., Wang, J., Chivers, P. T., & Codd, R. (2023). Reduction-cleavable desferrioxamine B pulldown system enriches Ni( ii )-superoxide dismutase from a Streptomyces proteome. RSC Chemical Biology, 4, Article 1064. https://doi.org/10.1039/d3cb00097d

Two resins with the hydroxamic acid siderophore desferrioxamine B (DFOB) immobilised as a free ligand or its Fe(iii) complex were prepared to screen the Streptomyces pilosus proteome for proteins involved in siderophore-mediated Fe(iii) uptake. The r... Read More about Reduction-cleavable desferrioxamine B pulldown system enriches Ni( ii )-superoxide dismutase from a Streptomyces proteome.

In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation (2023)
Journal Article
Basak, P., Cabelli, D. E., Chivers, P. T., Farquhar, E. R., & Maroney, M. J. (2023). In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation. Metallomics, 15(11), Article mfad054. https://doi.org/10.1093/mtomcs/mfad054

The importance of cellular low molecular weight (LMW) ligands in metalloenzyme maturation is largely unexplored. Maturation of NiSOD requires post-translational N-terminal processing of the proenzyme, SodN, by its cognate protease, SodX. Here we prov... Read More about In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation.

Protein metalation in biology (2021)
Journal Article
Foster, A. W., Young, T. R., Chivers, P. T., & Robinson, N. J. (2022). Protein metalation in biology. Current Opinion in Chemical Biology, 66, Article 102095. https://doi.org/10.1016/j.cbpa.2021.102095

Inorganic metals supplement the chemical repertoire of organic molecules, especially proteins. This requires the correct metals to associate with proteins at metalation. Protein mismetalation typically occurs when excesses of unbound metals compete f... Read More about Protein metalation in biology.

Bacterial sensors define intracellular free energies for correct enzyme metalation (2019)
Journal Article
Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J., Morton, R. J., Steed, J. W., Lurie-Luke, E., Huggins, T. G., Lawrence, A. D., Deery, E., Warren, M. J., Chivers, P. T., & Robinson, N. J. (2019). Bacterial sensors define intracellular free energies for correct enzyme metalation. Nature Chemical Biology, 15(3), 241-249. https://doi.org/10.1038/s41589-018-0211-4

There is a challenge for metalloenzymes to acquire their correct metals because some inorganic elements form more stable complexes with proteins than do others. These preferences can be overcome provided some metals are more available than others. Ho... Read More about Bacterial sensors define intracellular free energies for correct enzyme metalation.

Co(II) and Ni(II) binding of the Escherichia coli transcriptional repressor RcnR orders its N-terminus, alters helix dynamics, and reduces DNA affinity (2017)
Journal Article
Huang, H., Bobst, C., Iwig, J., Chivers, P., Kaltashov, I., & Maroney, M. (2018). Co(II) and Ni(II) binding of the Escherichia coli transcriptional repressor RcnR orders its N-terminus, alters helix dynamics, and reduces DNA affinity. Journal of Biological Chemistry, 293(1), 324-332. https://doi.org/10.1074/jbc.ra117.000398

RcnR, a transcriptional regulator in Escherichia coli, derepresses the expression of the export proteins RcnAB upon binding Ni(II) or Co(II). Lack of structural information has precluded elucidation of the allosteric basis for the decreased DNA affin... Read More about Co(II) and Ni(II) binding of the Escherichia coli transcriptional repressor RcnR orders its N-terminus, alters helix dynamics, and reduces DNA affinity.

Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR (2017)
Journal Article
Carr, C., Musiani, F., Huang, H., Chivers, P., Ciurli, S., & Maroney, M. (2017). Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR. Inorganic Chemistry, 56(11), 6459-6476. https://doi.org/10.1021/acs.inorgchem.7b00527

Escherichia coli RcnR (resistance to cobalt and nickel regulator, EcRcnR) is a metal-responsive repressor of the genes encoding the Ni(II) and Co(II) exporter proteins RcnAB by binding to PRcnAB. The DNA binding affinity is weakened when the cognate... Read More about Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR.

Elucidation of the biosynthesis of the methane catalyst coenzyme F430 (2017)
Journal Article
Moore, S., Sowa, S., Schuchardt, C., Deery, E., Lawrence, A., Ramos, J., …Warren, M. (2017). Elucidation of the biosynthesis of the methane catalyst coenzyme F430. Nature, 543(7643), 78-82. https://doi.org/10.1038/nature21427

Methane biogenesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible for the utilization of methane through anaerobic methane oxidation. The enzyme uses an ancillary factor called coenzyme F430, a nickel-co... Read More about Elucidation of the biosynthesis of the methane catalyst coenzyme F430.

A tight tunable range for Ni(II) sensing and buffering in cells (2017)
Journal Article
Foster, A., Pernil, R., Patterson, C., Scott, A., Pålsson, L., Pal, R., …Robinson, N. (2017). A tight tunable range for Ni(II) sensing and buffering in cells. Nature Chemical Biology, 13(4), 409-414. https://doi.org/10.1038/nchembio.2310

The metal affinities of metal-sensing transcriptional regulators co-vary with cellular metal concentrations over more than 12 orders of magnitude. To understand the cause of this relationship, we determined the structure of the Ni(II) sensor InrS and... Read More about A tight tunable range for Ni(II) sensing and buffering in cells.

The mechanism of a formaldehyde-sensing transcriptional regulator (2016)
Journal Article
Denby, K., Iwig, J., Bisson, C., Westwood, J., Rolfe, M., Sedelnikova, S., …Green, J. (2016). The mechanism of a formaldehyde-sensing transcriptional regulator. Scientific Reports, 6, Article 38879. https://doi.org/10.1038/srep38879

Most organisms are exposed to the genotoxic chemical formaldehyde, either from endogenous or environmental sources. Therefore, biology has evolved systems to perceive and detoxify formaldehyde. The frmRA(B) operon that is present in many bacteria rep... Read More about The mechanism of a formaldehyde-sensing transcriptional regulator.