ArticleJournal of the American Chemical Society2014
Anisotropic covalency contributions to superexchange pathways in type one copper active sites.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 77 citations in OpenAlex.
- The Long-Range High-pH Proton Channel Facilitates the Nitrite Reduction in Copper-Containing Nitrite Reductase.ACS omega · 2025Article
- Protein Quakes in Redox Metalloenzymes: Clues to Molecular Enzyme Conductivity Triggered by Binding of Small Substrate Molecules.ChemistryOpen · 2024Article
- Mutations of methionine 444 interacting with T1Cu-coordinating amino acids affect the structure and function of multicopper oxidase CopA.Biodegradation · 2024Article
- Tuning the Type 1 Reduction Potential of Multicopper Oxidases: Uncoupling the Effects of Electrostatics and H-Bonding to Histidine Ligands.Journal of the American Chemical Society · 2023Article
- Intense Photoinduced Intervalence Charge Transfer in High-Valent Iron Mixed Phenolate/Carbene Complexes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Spiers Memorial Lecture: activating metal sites for biological electron transfer.Faraday discussions · 2022Review
- Current status of neutron crystallography in structural biology.Biophysics and physicobiology · 2022Article
- Copper nitrite reductase from Sinorhizobium meliloti 2011: Crystal structure and interaction with the physiological versus a nonmetabolically related cupredoxin-like mediator.Protein science : a publication of the Protein Society · 2021Article
- Electron Transfer to the Trinuclear Copper Cluster in Electrocatalysis by the Multicopper Oxidases.Journal of the American Chemical Society · 2021Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- The three-spin intermediate at the O-O cleavage and proton-pumping junction in heme-Cu oxidases.Science (New York, N.Y.) · 2021Article
- Article
- High-resolution neutron crystallography visualizes an OH-bound resting state of a copper-containing nitrite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- OJournal of the American Chemical Society · 2019Article
- Mechanism of O2 activation and substrate hydroxylation in noncoupled binuclear copper monooxygenases.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Activating Metal Sites for Biological Electron Transfer.Israel journal of chemistry · 2016Article
- Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.Inorganic chemistry · 2016Review
- Two-Electron Reduction versus One-Electron Oxidation of the Type 3 Pair in the Multicopper Oxidases.Journal of the American Chemical Society · 2015Article
- Electron transfer and reaction mechanism of laccases.Cellular and molecular life sciences : CMLS · 2015Review
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Type one (T1) Cu sites deliver electrons to catalytic Cu active sites: the mononuclear type two (T2) Cu site in nitrite reductases (NiRs) and the trinuclear Cu cluster in the multicopper oxidases (MCOs). The T1 Cu and the remote catalytic sites are connected via a Cys-His intramolecular electron-transfer (ET) bridge, which contains two potential ET pathways: P1 through the protein backbone and P2 through the H-bond between the Cys and the His. The high covalency of the T1 Cu-S(Cys) bond is shown here to activate the T1 Cu site for hole superexchange via occupied valence orbitals of the bridge. This covalency-activated electronic coupling (H(DA)) facilitates long-range ET through both pathways. These pathways can be selectively activated depending on the geometric and electronic structure of the T1 Cu site and thus the anisotropic covalency of the T1 Cu-S(Cys) bond. In NiRs, blue (π-type) T1 sites utilize P1 and green (σ-type) T1 sites utilize P2, with P2 being more efficient. Comparing the MCOs to NiRs, the second-sphere environment changes the conformation of the Cys-His pathway, which selectively activates HDA for superexchange by blue π sites for efficient turnover in catalysis. These studies show that a given protein bridge, here Cys-His, provides different superexchange pathways and electronic couplings depending on the anisotropic covalencies of the donor and acceptor metal sites.
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