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A Bis(imidazole)-based cysteine labeling tool for metalloprotein assembly

https://doi.org/10.1016/j.jinorgbio.2023.112206

Ahmad, Raheel; Tyryshkin, Alexei M; Xie, Lingjun; Hansen, William A; Yachnin, Brahm J; Emge, Thomas J; Mashrai, Ashraf; Khare, Sagar D; Knapp, Spencer (July 2023, Journal of Inorganic Biochemistry)

Precise metal-protein coordination by design remains a considerable challenge. Polydentate, high-metal-affinity protein modifications, both chemical and recombinant, can enable metal localization. However, these constructs are often bulky, conformationally and stereochemically ill-defined, or coordinately saturated. An X-ray protein crystal structure of BMIE-modified CPG2-S203C demonstrates that the BMIE modification is minimally disruptive to the overall protein structure, including the carboxypeptidase active sites, although Zn++ metalation could not be conclusively discerned at the resolution obtained.
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A redox-active Mn(0) dicarbene metalloradical

https://doi.org/10.1039/D2CC04677F

Karagiannis, Ageliki; Tyryshkin, Alexei M.; Lalancette, Roger A.; Spasyuk, Denis M.; Washington, Asmaa; Prokopchuk, Demyan E. (November 2022, Chemical Communications)

A rare redox-active Mn(0) dicarbene anion with solvent-dependent electrochemical behaviour has been synthesized and thoroughly characterized.
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Design of a minimal di-nickel hydrogenase peptide

https://doi.org/10.1126/sciadv.abq1990

Timm, Jennifer; Pike, Douglas H.; Mancini, Joshua A.; Tyryshkin, Alexei M.; Poudel, Saroj; Siess, Jan A.; Molinaro, Paul M.; McCann, James J.; Waldie, Kate M.; Koder, Ronald L.; et al (March 2023, Science Advances)
Thorp, Holden (Ed.)
Ancestral metabolic processes involve the reversible oxidation of molecular hydrogen by hydrogenase. Extant hydrogenase enzymes are complex, comprising hundreds of amino acids and multiple cofactors. We designed a 13–amino acid nickel-binding peptide capable of robustly producing molecular hydrogen from protons under a wide variety of conditions. The peptide forms a di-nickel cluster structurally analogous to a Ni-Fe cluster in [NiFe] hydrogenase and the Ni-Ni cluster in acetyl-CoA synthase, two ancient, extant proteins central to metabolism. These experimental results demonstrate that modern enzymes, despite their enormous complexity, likely evolved from simple peptide precursors on early Earth.
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Design of a Fe ₄ S ₄ cluster into the core of a de novo four‐helix bundle

https://doi.org/10.1002/bab.2003

Mancini, Joshua A.; Pike, Douglas H.; Tyryshkin, Alexei M.; Haramaty, Liti; Wang, Michael S.; Poudel, Saroj; Hecht, Michael; Nanda, Vikas (July 2020, Biotechnology and Applied Biochemistry)
null (Ed.)
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Observation of an environmentally insensitive solid-state spin defect in diamond

https://doi.org/10.1126/science.aao0290

Rose, Brendon C.; Huang, Ding; Zhang, Zi-Huai; Stevenson, Paul; Tyryshkin, Alexei M.; Sangtawesin, Sorawis; Srinivasan, Srikanth; Loudin, Lorne; Markham, Matthew L.; Edmonds, Andrew M.; et al (July 2018, Science)