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Maurizio Bruschi

Researcher at University of Milano-Bicocca

Publications -  18
Citations -  1722

Maurizio Bruschi is an academic researcher from University of Milano-Bicocca. The author has contributed to research in topics: Active site & Catalysis. The author has an hindex of 17, co-authored 18 publications receiving 1643 citations. Previous affiliations of Maurizio Bruschi include University of Milan & Mario Negri Institute for Pharmacological Research.

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Synthesis of the H-cluster framework of iron-only hydrogenase

TL;DR: The assembly of the iron-sulphur framework of the active site of iron-only hydrogenase (the H-cluster) is reported, and it is shown that it functions as an electrocatalyst for proton reduction.
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DFT investigations of models related to the active site of [NiFe] and [Fe] hydrogenases

TL;DR: In this article, the role of theoretical contributions in the investigation of synthetic models related to the enzymatic metal cofactors is discussed, showing how ‘in silico’ coordination chemistry can nicely complement experimental studies in the characterization of relevant species.
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A QM/MM investigation of the activation and catalytic mechanism of Fe-only hydrogenases

TL;DR: The investigation of a catalytic cycle of the Fe-only hydrogenase that implies formation of a terminal hydride ion and a di(thiomethyl)amine (DTMA) molecule acting as an acid/base catalyst indicates that all steps have reasonable reaction energies and that the influence of the protein on the thermodynamic profile of H(2) production catalysis is not negligible.
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Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126.

TL;DR: Amyloid fibrils are not required for neurotoxicity because the effects of PrP106-126 NH(2) on primary neuronal cultures were similar to those of the wild-type sequence, suggesting that astrogliosis in prion encephalopathies without amyloid deposits is a mediated effect rather than a direct effect of disease-specific PrP isoforms.
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Investigations on the role of proton-coupled electron transfer in hydrogen activation by [FeFe]-hydrogenase.

TL;DR: Spectra associated with Hred and Hsred states are less populated in the Cys → Ser variant, demonstrating that the exchange of -SH with -OH alters how the H-cluster equilibrates among different reduced states of the catalytic cycle under steady-state conditions.