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Role of Hydrogen Bond Connecting Ligands for Substrate and Type I Copper in Copper(I) Oxidase CueO
14/14 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
2 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 14 checked references that resolve
resolves10.1074/jbc.M104122200
The Independent cue and cusSystems Confer Copper Tolerance during Aerobic and Anaerobic Growth inEscherichia coli
resolves10.1128/JB.186.17.5826-5833.2004
Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in
<i>Escherichia coli</i>
resolves10.1002/tcr.20125
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
resolves10.1016/j.jmb.2007.07.041
Structure and Function of the Engineered Multicopper Oxidase CueO from Escherichia coli—Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site
resolves10.1074/jbc.M808468200
Four-electron Reduction of Dioxygen by a Multicopper Oxidase, CueO, and Roles of Asp112 and Glu506 Located Adjacent to the Trinuclear Copper Center
resolves10.1021/bi101107c
Enhancement of Laccase Activity through the Construction and Breakdown of a Hydrogen Bond at the Type I Copper Center in <i>Escherichia coli</i> CueO and the Deletion Mutant Δα5−7 CueO
resolves10.1002/anie.201107739
An O‐Centered Structure of the Trinuclear Copper Center in the Cys500Ser/Glu506Gln Mutant of CueO and Structural Changes in Low to High X‐Ray Dose Conditions
resolves10.1007/s007750050156
An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity
resolves10.1021/ja049220t
Ferrous Binding to the Multicopper Oxidases<i>Saccharomyces c</i><i>erevisiae</i>Fet3p and Human Ceruloplasmin: Contributions to Ferroxidase Activity
resolves10.1128/JB.183.16.4866-4875.2001
Oxidation of Phenolate Siderophores by the Multicopper Oxidase Encoded by the<i>Escherichia coli yacK</i>Gene
resolves10.1128/JB.186.22.7815-7817.2004
Cuprous Oxidase Activity of CueO from
<i>Escherichia coli</i>
resolves10.1016/j.bbrc.2012.04.127
Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities
resolves10.1074/jbc.M302963200
A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase CueO
The 2 references without a DOI — listed, not checked
no DOI — not checked2024011812092073600_r5
no DOI — not checked2024011812092073600_r13
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