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N₂ O Reductase Activity of a [Cu₄ S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere.

ABSTRACT: The model complex [Cu₄ (μ₄ -S)(dppa)₄ ]²⁺ (1, dppa=μ₂ -(Ph₂ P)₂ NH) has N₂ O reductase activity in methanol solvent, mediating 2 H⁺ /2 e^- reduction of N₂ O to N₂ +H₂ O in the presence of an exogenous electron donor (CoCp₂ ). A stoichiometric product with two deprotonated dppa ligands was characterized, indicating a key role of second-sphere N-H residues as proton donors during N₂ O reduction. The activity of 1 towards N₂ O was suppressed in solvents that are unable to provide hydrogen bonding to the second-sphere N-H groups. Structural and computational data indicate that second-sphere hydrogen bonding induces struct

SUBMITTER: Hsu CW

PROVIDER: S-EPMC6940516 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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N₂ O Reductase Activity of a [Cu₄ S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere.

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N2 O Reductase Activity of a [Cu4 S] Cluster in the 4CuI Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere.

OmicsDI is part of the ELIXIR infrastructure

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N₂ O Reductase Activity of a [Cu₄ S] Cluster in the 4Cu^I Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere.