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Kinetic and Thermodynamic Analysis of Cu2+-Dependent Reductive Inactivation in Direct Electron Transfer-Type Bioelectrocatalysis by Copper Efflux Oxidase

https://doi.org/10.2139/ssrn.4102755
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27/27 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.

6 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 27 checked references that resolve
resolves10.1021/cr950046o
Multicopper Oxidases and Oxygenases
resolves10.1002/tcr.20125
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
resolves10.1098/rsif.2017.0253
Direct enzymatic bioelectrocatalysis: differentiating between myth and reality
resolves10.1002/chem.201800750
Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
resolves10.1016/j.coelec.2017.08.005
New perspectives in hydrogenase direct electrochemistry
resolves10.1016/j.electacta.2021.138836
Some fundamental insights into biological redox catalysis from the electrochemical characteristics of enzymes attached directly to electrodes
resolves10.3390/s18051319
Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells
resolves10.1021/acs.chemrev.7b00220
O<sub>2</sub>Reduction in Enzymatic Biofuel Cells
resolves10.1016/j.jelechem.2020.113895
Diffusion-limited biosensing of dissolved oxygen by direct electron transfer-type bioelectrocatalysis of multi-copper oxidases immobilized on porous gold microelectrodes
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
resolves10.1246/cl.2007.232
Promotion of Laccase Activities of <i>Escherichia coli</i> Cuprous Oxidase, CueO by Deleting the Segment Covering the Substrate Binding Site
resolves10.1074/jbc.M302963200
A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase CueO
resolves10.1074/jbc.M111.293589
Crystal Structures of Multicopper Oxidase CueO Bound to Copper(I) and Silver(I)
resolves10.1246/cl.2007.132
Bioelectrocatalytic Reduction of O2 Catalyzed by CueO from <i>Escherichia coli</i> Adsorbed on a Highly Oriented Pyrolytic Graphite Electrode
resolves10.5796/electrochemistry.20-00015
Effects of Elimination of α Helix Regions on Direct Electron Transfer-type Bioelectrocatalytic Properties of Copper Efflux Oxidase
resolves10.1021/jacs.9b11147
Interplay between Orientation at Electrodes and Copper Activation of <i>Thermus thermophilus</i> Laccase for O<sub>2</sub> Reduction
resolves10.1016/j.jbiotec.2016.04.035
Increasing the catalytic activity of Bilirubin oxidase from Bacillus pumilus: Importance of host strain and chaperones proteins
resolves10.1021/cr050191u
Investigating and Exploiting the Electrocatalytic Properties of Hydrogenases
resolves10.1016/j.jelechem.2016.02.009
Bioelectrochemical analysis of thermodynamics of the catalytic cycle and kinetics of the oxidative inactivation of oxygen-tolerant [NiFe]-hydrogenase
resolves10.1073/pnas.1212258109
Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants
resolves10.1021/cr60231a002
Diffusion of Dissolved Gases in Liquids
resolves10.1063/1.555562
Viscosity of water substance—new international formulation and its background
resolves10.1016/0005-2744(72)90074-5
The use of dixon plots to study enzyme inhibition
resolves10.1016/j.abb.2018.06.009
The many faces of partial inhibition: Revealing imposters with graphical analysis
resolves10.1246/cl.130422
Role of Hydrogen Bond Connecting Ligands for Substrate and Type I Copper in Copper(I) Oxidase CueO
resolves10.1039/b800799c
O2 Reduction to H2O by the multicopper oxidases
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
The 6 references without a DOI — listed, not checked
no DOI — not checkedCopper homeostatic mechanisms and their role in the virulence of Escherichia coli and Salmonella enterica
no DOI — not checkedref11
no DOI — not checkedStandard potential in aqueous solution
no DOI — not checkedA study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
no DOI — not checkedOxygen and Ozone
no DOI — not checkedCrystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

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