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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.
This study presents a microorganism electrocatalyst for the cathode of a microbial fuel cell that allows simultaneous electricity generation and treatment of sewage.
Human manganese superoxide dismutase is an oxidoreductase that converts superoxide to molecular oxygen and hydrogen peroxide with proton-coupled electron transfers (PCETs), and has evolved to be highly product inhibited to limit the formation of hydrogen peroxide. Here, the authors use neutron diffraction and X-ray absorption spectroscopy of the product-bound, trivalent, and divalent states of the enzyme to identify the product-inhibited complex and propose a PCET mechanism.
Despite the progression of Actinium-225 (225Ac) radiopharmaceuticals, there is still a limited understanding of Ac coordination chemistry due to its radioactivity, poor availability, and lack of stable isotopes. Here, the authors demonstrate a platform to characterize the solution and solid-state behavior of the longest-lived Ac isotope, 227Ac.
Despite the significance of H2O2-metal adducts, the nature of the interactions between H2O2 and metal cations remains elusive due to the weak coordinating ability of H2O2, which poses challenges in characterizing the specific nature of these interactions. Herein, the authors obtain H2O2–metal complexes using H2O2 as both solvent and ligand.
Biological nitrogen fixation requires low-potential electrons from ferredoxin or flavodoxin. Here the authors show how the soil diazotroph Azotobacter vinelandii employs the NADH:ferredoxin oxidoreductase RNF1 complex to lower the midpoint potential of the electron from NADH to reduce ferredoxin.
Soluble methane monooxygenase (sMMO) is a potentially value biocatalyst, but production of active recombinant sMMO is very challenging. Here the authors report the rational design and construction of a catalytically active miniature sMMO which enables high-yield production of methanol in E. coli.
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.