Staff profile

• bacteriology
• bioinorganic chemistry
• biotechnology
• metalloproteins
• microbiology
• nickel
• protein chemistry
• protein engineering

Chapter in book

• Chivers, P. (2012). Urease and the bacterial acid-stress response. In Stress Response in Pathogenic Bacteria (167-181). CABI Publishing

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
• Ni, J., Wood, J. L., White, M. Y., Lihi, N., Markham, T. E., Wang, J., …Codd, R. (2023). Reduction-cleavable desferrioxamine B pulldown system enriches Ni( ii )-superoxide dismutase from a Streptomyces proteome. RSC Chemical Biology, https://doi.org/10.1039/d3cb00097d
• 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
• Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J., Morton, R. J., …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
• 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
• 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
• 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
• 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
• 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
• Chivers, P. (2015). Nickel recognition by bacterial importer proteins. Metallomics, 7(4), 590-595. https://doi.org/10.1039/c4mt00310a
• Higgins, K., Hu, H., Chivers, P., & Maroney, M. (2013). The Effects of Select Histidine to Cysteine Mutations on Transcriptional Regulation by E. coli RcnR. Biochemistry, 52(1), 84-97. https://doi.org/10.1021/bi300886q
• Chivers, P., Benanti, E., Heil-Chapdelaine, V., Iwig, J., & Rowe, J. (2012). Identification of Ni-(L-His)2 as a substrate for NikABCDE-dependent nickel uptake in Escherichia coli. Metallomics, 4(10), 1043 -1050. https://doi.org/10.1039/c2mt20139a
• Higgins, K., Chivers, P., & Maroney, M. (2012). Role of the N-terminus in determining metal-specific responses in the E. coli Ni- and Co-responsive metalloregulator, RcnR. Journal of the American Chemical Society, 134(16), 7081-7093. https://doi.org/10.1021/ja300834b
• Benanti, E., & Chivers, P. (2011). Helicobacter pylori NikR Protein Exhibits Distinct Conformations When Bound to Different Promoters. Journal of Biological Chemistry, 286(18), 15728-15737. https://doi.org/10.1074/jbc.m110.196055
• Choi, S., Chivers, P., & Berg, D. (2011). Point mutations in Helicobacter pylori's fur regulatory gene that alter resistance to metronidazole, a prodrug activated by chemical reduction. PLoS ONE, 6(3), https://doi.org/10.1371/journal.pone.0018236
• Benanti, E., & Chivers, P. (2010). Geobacter uraniireducens NikR displays a DNA binding mode distinct from other members of the NikR family. Journal of Bacteriology, 192(17), 4327-4336. https://doi.org/10.1128/jb.00152-10
• Herbst, R., Perovic, I., O'Brien, K., Chivers, P., Pochapsky, S., Pochapsky, T., & Maroney, M. (2010). The communication between the zinc and nickel sites in dimeric HypA: Metal recognition and pH sensing. Journal of the American Chemical Society, 132(30), https://doi.org/10.1021/ja1005724
• Iwig, J., & Chivers, P. (2010). Coordinating intracellular nickel – metal-site structure-function relationships and the NikR and RcnR repressors. Natural Product Reports, 27(5), 658-667. https://doi.org/10.1039/b906683g
• Iwig, J., & Chivers, P. (2009). DNA Recognition and Wrapping by Escherichia coli RcnR. Journal of Molecular Biology, 393(2), https://doi.org/10.1016/j.jmb.2009.08.038
• Benanti, E., & Chivers, P. (2009). An intact urease assembly pathway is required to compete with NikR for nickel ions in Helicobacter pylori. Journal of Bacteriology, 191(7), 2405-2408. https://doi.org/10.1128/jb.01657-08
• Iwig, J., Leitch, S., Herbst, R., Maroney, M., & Chivers, P. (2008). Ni(II) and Co(II) sensing by Escherichia coli RcnR. Journal of the American Chemical Society, 130(24), https://doi.org/10.1021/ja710067d
• Bradley, M., Chivers, P., & Baker, N. (2008). Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways. Journal of Molecular Biology, 378(5), 1155-1173. https://doi.org/10.1016/j.jmb.2008.03.010
• Kennedy, D., Herbst, R., Iwig, J., Chivers, P., & Maroney, M. (2007). A Dynamic Zn Site in Helicobacter pylori HypA: A Potential Mechanism for Metal-Specific Protein Activity. Journal of the American Chemical Society, 129(1), https://doi.org/10.1021/ja066958x
• Chivers, P. (2007). A Galvanizing Story – Protein Stability and Zinc Homeostasis. Journal of Bacteriology, 189(8), 2953-2954. https://doi.org/10.1128/jb.00173-07
• Leitch, S., Bradley, M., Rowe, J., Chivers, P., & Maroney, M. (2007). Nickel-specific response in the transcriptional regulator, Escherichia coli NikR. Journal of the American Chemical Society, 129(16), 5085-5095. https://doi.org/10.1021/ja068505y
• Benanti, E., & Chivers, P. (2007). The N-terminal arm of the Helicobacter pylori Ni2+-dependent transcription factor NikR is required for specific DNA binding. Journal of Biological Chemistry, 282(28), https://doi.org/10.1074/jbc.m702982200
• Iwig, J., Rowe, J., & Chivers, P. (2006). Nickel homeostasis in Escherichia coli – the rcnR-rcnA efflux pathway and its linkage to NikR function. Molecular Microbiology, 62(1), https://doi.org/10.1111/j.1365-2958.2006.05369.x
• Rowe, J., Starnes, G., & Chivers, P. (2005). Complex transcriptional control links NikABCDE-dependent nickel transport with hydrogenase expression in Escherichia coli. Journal of Bacteriology, 187(18), 6317-6323. https://doi.org/10.1128/jb.187.18.6317-6323.2005