Themed collection Nickel in biology

This editorial introduces the Nickel in Biology themed issue for Metallomics, guest edited by Deborah Zamble.

The application of metals in medicine has evolved over the years since the days of alchemists to the present novel concept of catalytic metallodrugs with nuclease and protease activity. It is projected that in the near future catalytic metallodrugs should play key roles in the emerging area of personalized medicine.

The structural features, metal coordination modes and metal binding thermodynamics of known Ni(II)-dependent transcriptional regulators are highlighted and discussed.

Nickel recognition for microbial import exhibits coordination features distinct from other cellular functions.

Analytical strategies to study the nickel proteome and their advantages and limitations.

Nickel inhibits microbial enzymes (substituting for the normal metal or binding to catalytic/secondary sites) and indirectly creates reactive oxygen species.

HpSlyD interacts with HpHypB through its insert-in-flap (IF) domain and delivers Ni²⁺ to HpHypB, which induces the dimerization of HpHypB and enhances its GTPase activity.

In Rhodospirillum rubrum, maturation of Carbon Monoxide Dehydrogenase (CODH) requires three accessory proteins, CooC, CooT and CooJ, dedicated to nickel insertion into the active site, which constitutes a distorted [NiFe₃S₄] cubane coordinated with a mononuclear Fe site.

SlyD activates the release of nickel and blocks the release of zinc from the high-affinity metal site of HypB.

“Metal-tunable” fluorescent probe for tracking and editing metalloproteomes inside living cells.

Combinatorial genome-wide analyses of transcriptome changes in response to genetic mutation and environmental perturbations give insight into a network of oxygen, copper and nickel signaling.

Novel Ni-coordination in a [NiFe]-hydrogenase mutant and possible coexistence of hydride and sulfenic acid in the WT Ni-SI_b state.

In Cupriavidus metallidurans disturbed metal homeostasis silences catabolic metabolic genomic islands (CMGIs) containing genes for nickel-dependent hydrogenases. This situation is reverted in a ΔzupT mutant.

In nickel-tolerant Streptomyces coelicolor, a highly nickel-sensitive regulator (Nur) for nickel uptake systems and an extremely insensitive regulator (NmtR) for a nickel efflux pump constitute the nickel homeostasis system.

Functional and topological analysis of Rhizobium leguminosarum HupE, the founding member of the HupE/UreJ family of nickel permeases, provides new hints on how bacteria manage nickel provision for metalloenzyme synthesis.

The metallochaperone SlyD is essential for nickel delivery to hydrogenase in stationary phase E. coli cells.

Atomic-resolution structures illustrate how Ni(II) sensing by CnrXs proceeds by conformational selection to prime signal propagation.

Staphylococcus aureus possesses two canonical ABC-importers dedicated to nickel acquisition: the NikABCDE and the CntABCDF systems, active under different growth conditions.

HypA structural Zn site mutants affect acid survival of Helicobacter pylori.

Ni(II) ions cleave AAT hydrolytically, inactivating the protein.

Switching between the two metal activation classes of glyoxalase I by protein engineering using deletional mutagenesis.

The Helicobacter pylori transcription factor NikR represses two novel gene targets in a nickel-dependent manner.

Nickel homeostasis in Haemophilus influenzae is tightly coupled to planktonic-sessile lifestyle switch.

Direct in vitro and in vivo evidence as well as molecular details of nickel translocation mediated by HypA–UreE interaction.

Biochemical characterization of a P_1B-5-ATPase suggests that this subfamily is involved in Ni²⁺ and Fe²⁺ transport.

Cobalt and nickel metalloproteome is involved in protein metabolism, carbonhydrate metabolism and gene expression regulation. Co- and Ni-binding motifs H(X)nH, M(X)nH and H(X)nM are identified.

Nickel and cobalt are obligate nutrients for the gammaproteobacteria but when present at high concentrations they display toxic effects.

The results described here identify the first nickel complex, Ni-(L-His)₂, that is imported by microbes.

Nickel increases the current activated by glutamate in NMDA receptors containing the subunit GluN2B and this potentiation is dependent on external Ca²⁺ demonstrating that divalent cations influence each other in the modulation of NMDA receptor function.

The novel MerR-like regulator NimR from Haemophilus influenzae regulates nickel uptake and this controls urease activity.