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Metalloproteins are proteins bound by at least one metal ion. Metal ions are usually coordinated by four sites consisting of the protein’s nitrogen, sulphur and/or oxygen atoms. In metalloenzymes, one of the coordination sites is labile. The chemistry of metals allows for a broader set of reactions, for instance as in redox reactions.
The biogenesis of iron-sulfur proteins in eukaryotes is initiated by the mitochondrial core ISC complex. Here, the authors provide structural, biochemical and spectroscopic data to characterize sulfur transfer intermediates in the core ISC complex.
Heme is an abundant cofactor required by nearly all known organisms. Here, authors discover a cyanobacterial protein with a distinct Zn-mirror heme site, which may function to sense heme and regulate energy metabolism.
How do cells put electrons to rest? Using a minimal pathway to get rid of excess metabolic electrons, diverse environmentally important microbes overcome large spatial, kinetic, and thermodynamic barriers in order to survive in extreme anoxic conditions.
NinaB is an isomerooxygenase that generates visual chromophore (11-cis-retinal) from carotenoid substrates. Here Solano et al. reveal the structural basis for NinaB isomerase activity, providing new insights into the evolution of visual chromophore synthesis by carotenoid cleavage enzymes.
The inorganic minerals are believed to exert a critical catalytic role in the prebiotic time, but biominerals (e.g., bones) in modern living organisms are known mainly for their physical property-related functions. Here the authors identify natural ferritin iron core as a superoxide dismutase-like nanozyme exhibiting species-related activity and elucidate its specific catalytic mechanism.
Protein stability is important for biological function, but little is known about in-cell stability. In the New Delhi metallo-β-lactamase NDM-1, enhancement of zinc binding or amino acid substitutions at the C terminus increase in-cell kinetic stability and prevent proteolysis. These findings link NDM-1-mediated resistance with its in-cell stability and physiology.
The combination of mass spectroscopy-based proteomics with molecular dynamics enables the in-depth study of metallothioneine-Zn(II) binding mechanisms, critical to cell homeostasis and Zn(II) ion buffering.
The ability to control the subtle differences in reaction mechanisms and outcomes is an aspiration of many synthetic chemists. Now protein evolution has enabled the control of selectivity for hydroamination reactions catalysed by gold-based artificial metalloenzymes by favouring dual-gold catalysis over monomeric catalysis.
