Bacterial glyoxalase I enzymes: structural and biochemical investigations

Honek, John F.

doi:10.1042/bst20130285

Cited by 6 publications

(5 citation statements)

References 50 publications

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“…Eight enzymatic systems are accepted as having capability and selectivity for Ni(II) binding, 100 three of which have an isolated, monomeric Ni(II) ion. Two of these three (bacterial glyoxylase I 101 and acireductone dioxygenase (ARD)) 100 coordinate in highspin octahedral geometry, analogous to the gas-phase CS binding mode discussed here. The third of these, superoxide dismutase (SOD), uses two cysteine sulfur chelation points along with imidazole nitrogens to form a low-spin square-planar site.…”

Section: Discussionmentioning

confidence: 78%

Complexes of Ni(ii) and Cu(ii) with small peptides: deciding whether to deprotonate

Dunbar

Martens

Berden

2016

Phys. Chem. Chem. Phys.

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The observed variety of metal-ion complexation sites offered by peptides reflects a basic tension between charge solvation of the ion by Lewis-basic chelating groups versus amide nitrogen deprotonation and formation of metal-nitrogen bonds. Gas-phase models of metal-ion coordination can illuminate the factors governing this choice in condensed-phase proteins and enzymes. Here, structures of gas-phase complexes of Ni(ii) and Cu(ii) with tri- and tetra-peptide ligands are mapped out using a combination of Infrared Multiple Photon Dissociation (IRMPD) spectroscopy and density functional theory (DFT) computations. The two binding modes give distinctive IRMPD signatures, particularly in the diagnostic region 1500-1550 cm. Previous observations have suggested that Ni(ii) complexes preferentially show the iminol rearrangement pattern (Im) giving low-spin square-planar geometries with metal-ion bonds to deprotonated amide nitrogens. In contrast, alkaline earth metal ion complexes prefer amide carbonyl oxygens chelating the metal ion with pyramidal geometry (charge-solvation, CS). Surprisingly, it is shown here that the Gly complexes are CS bound, in contrast with the expectation of Im binding. It is suggested that CS binding is actually a normal Ni(ii) and Cu(ii) binding mode to simple peptides lacking participating side chains. Three factors are suggested to influence the choice between CS and Im binding patterns: (1) presence of an accessible side-chain Lewis-basic proton interaction site (FGGF, FGG and HAA complexes); (2) short chain length of the peptide leading to a shortage of accessible carbonyl oxygen sites for CS binding, (AAA, FGG and HAA complexes); (3) outright deprotonation of the ligand giving net negatively charged Im[Ni(Gly-3H)] and Im[Ni(Ala-3H)] complexes, which have a triply-deprotonated ligand. IRMPD spectra of [CuGly] and [Cu(Gly-3H)] complexes suggest that their structures are similar to their Ni analogs.

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Section: Discussionmentioning

confidence: 78%

Complexes of Ni(ii) and Cu(ii) with small peptides: deciding whether to deprotonate

Dunbar

Martens

Berden

2016

Phys. Chem. Chem. Phys.

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“…Met-Seq hits PA0709 and PA3390, both ABM domains, were shown to bind heme directly and were found adjacent to or within operons that detoxify glyoxal (Fig. 8), a metabolite by-product of glycolysis and other pathways that can be damaging to cells, both prokaryotic and eukaryotic (109,125,126). These two novel ABM domains were unable to degrade heme, as most known heme-binding ABM domains have been shown to do in other pathogens; therefore, their precise functional roles remain to be determined.…”

Section: Discussionmentioning

confidence: 99%

“…Both of these genes are ABM domains, some of which have been implicated in the catabolism of heme in Staphylococcus aureus (106), Mycobacterium tuberculosis (107), and many other microbes (108). Interestingly, both PA3390 and PA0709 are transcriptionally linked to glyoxal detoxification enzymes (109,110), possibly suggesting a functional connection to the presence of this ubiquitous toxin (Fig. 8A).…”

Section: Genesmentioning

confidence: 99%

A High-Throughput Method for Identifying Novel Genes That Influence Metabolic Pathways Reveals New Iron and Heme Regulation in Pseudomonas aeruginosa

et al. 2021

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“…In the case of glutathione, the metalloenzyme Glyoxalase I, 59 24 common characteristics. Clearly the "simple" investigation of the biological chemistry of the carbon sulfur bond has led to numerous investigations that impact our knowledge of cellular function and health.…”

Section: Other Biological Systems Involving the Carbon-sulfur Bondmentioning

confidence: 99%

Biological chemistry of the carbon–sulfur bond

Honek

2015

Can. J. Chem.

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Carbon–sulfur biological chemistry encompasses a fascinating area of biochemistry and medicinal chemistry and includes the roles that methionine and S-adenosyl-l-methionine play in cells as well as the chemistry of intracellular thiols such as glutathione. This article, based on the 2014 Bernard Belleau Award lecture, provides an overview of some of the key investigations that were undertaken in this area from a bioorganic perspective. The research has ameliorated our fundamental knowledge of several of the enzymes utilizing these sulfur-containing molecules, has led to the development of several novel 19F biophysical probes, and has explored some of the medicinal chemistry associated with these processes.

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Bacterial glyoxalase I enzymes: structural and biochemical investigations

Cited by 6 publications

References 50 publications

Complexes of Ni(ii) and Cu(ii) with small peptides: deciding whether to deprotonate

Complexes of Ni(ii) and Cu(ii) with small peptides: deciding whether to deprotonate

A High-Throughput Method for Identifying Novel Genes That Influence Metabolic Pathways Reveals New Iron and Heme Regulation in Pseudomonas aeruginosa

Biological chemistry of the carbon–sulfur bond

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