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While they offer the advantages of operating under mild conditions and near-neutral pH, high reaction rates can profoundly alter the immobilized enzyme microenvironment. This requires understanding the interplay between localized concentration gradients and enzyme activity at the electrocatalytic interface. Here, we elucidate this dynamic coupling between reaction kinetics and local pH at an enzyme-modified electrode through a combined modeling and experimental approach. We present a detailed 2D-axisymmetric finite element model of a graphite microelectrode modified with bilirubin oxidase from Myrothecium verrucaria catalyzing the oxygen reduction reaction via direct electron transfer. The model explicitly accounts for buffer equilibria through ion activities and incorporates experimentally determined pH-dependent kinetic parameters, including apparent turnover and Michaelis constants. The simulations were validated experimentally using in situ and operando fluorescence confocal laser scanning microscopy (FCLSM) with the pH-sensitive dye fluorescein in weakly buffered electrolytes. Both numerical and experimental results reveal substantial interfacial alkalinization, with the local pH increasing by more than two units under the weakest buffering conditions. The model successfully reproduces cyclic voltammetry and quasi-steady-state chronoamperometry profiles using a single enzyme-coverage-dependent parameter. Furthermore, spatial fluorescence profiling closely corroborates the simulated pH gradients, while revealing evidence of natural convection occurring over extended time scales. Our study provides a quantitative framework crucial for designing stable, high-performance bioelectrochemical interfaces, which can be readily extended to other key redox enzymes, particularly those involved in CO2 and H2 conversion.<\/jats:p>","DOI":"10.1021\/jacs.6c15657","type":"journal-article","created":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T11:02:01Z","timestamp":1791457321000},"page":"45005-45018","source":"Crossref","is-referenced-by-count":0,"title":["Mapping and Modeling\nInterfacial pH Dynamics at Enzymatic\nMicroelectrode"],"prefix":"10.1021","volume":"148","author":[{"given":"Ruoyi","family":"Liu","sequence":"first","affiliation":[{"name":"CNRS, Aix Marseille University, BIP, Laboratoire de Bioe\u0301nerge\u0301tique et Inge\u0301nierie des Prote\u0301ines , 31 Chemin Joseph Aiguier , ,","place":["Marseille, France, 13402"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayaka","family":"Nishida","sequence":"additional","affiliation":[{"name":"Kyoto University , , Kitashirakawa Oiwake-cho, Sakyo-ku , ,","place":["Kyoto, Japan, 606-8502"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ami","family":"Kobayashi","sequence":"additional","affiliation":[{"name":"Kyoto University , , Kitashirakawa Oiwake-cho, Sakyo-ku , ,","place":["Kyoto, Japan, 606-8502"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9767-4922","authenticated-orcid":true,"given":"Keisei","family":"Sowa","sequence":"additional","affiliation":[{"name":"Kyoto University , , Kitashirakawa Oiwake-cho, Sakyo-ku , ,","place":["Kyoto, Japan, 606-8502"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2593-4670","authenticated-orcid":true,"given":"Elisabeth","family":"Lojou","sequence":"additional","affiliation":[{"name":"CNRS, Aix Marseille University, BIP, Laboratoire de Bioe\u0301nerge\u0301tique et Inge\u0301nierie des Prote\u0301ines , 31 Chemin Joseph Aiguier , ,","place":["Marseille, France, 13402"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0982-2209","authenticated-orcid":true,"given":"Anne","family":"de Poulpiquet","sequence":"additional","affiliation":[{"name":"CNRS, Aix Marseille University, BIP, Laboratoire de Bioe\u0301nerge\u0301tique et Inge\u0301nierie des Prote\u0301ines , 31 Chemin Joseph Aiguier , ,","place":["Marseille, France, 13402"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2563-3130","authenticated-orcid":true,"given":"Ievgen","family":"Mazurenko","sequence":"additional","affiliation":[{"name":"CNRS, Aix Marseille University, BIP, Laboratoire de Bioe\u0301nerge\u0301tique et Inge\u0301nierie des Prote\u0301ines , 31 Chemin Joseph Aiguier , ,","place":["Marseille, France, 13402"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,8]]},"reference":[{"issue":"16","key":"2026102111101881600_cit1","doi-asserted-by":"publisher","first-page":"9509","DOI":"10.1021\/acs.chemrev.9b00115","article-title":"Tackling the Challenges of Enzymatic (Bio)Fuel Cells","volume":"119","author":"Xiao","year":"2019","journal-title":"Chem. Rev."},{"key":"2026102111101881600_cit2","doi-asserted-by":"publisher","first-page":"100649","DOI":"10.1016\/j.coelec.2020.100649","article-title":"Measuring Local\npH in Electrochemistry","volume":"25","author":"Monteiro","year":"2021","journal-title":"Curr. Opin. Electrochem."},{"issue":"33","key":"2026102111101881600_cit3","doi-asserted-by":"publisher","first-page":"27377","DOI":"10.1021\/acsami.7b07351","article-title":"Spectroscopic Evidence of Size-Dependent\nBuffering\nof Interfacial pH by Cation Hydrolysis during CO2 Electroreduction","volume":"9","author":"Ayemoba","year":"2017","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"40","key":"2026102111101881600_cit4","doi-asserted-by":"publisher","first-page":"15891","DOI":"10.1021\/jacs.9b07000","article-title":"In Situ\nInfrared Spectroscopy Reveals Persistent Alkalinity\nnear Electrode Surfaces during CO2 Electroreduction","volume":"141","author":"Yang","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"10","key":"2026102111101881600_cit5","doi-asserted-by":"publisher","first-page":"3101","DOI":"10.1021\/acsenergylett.0c01606","article-title":"pH Matters\nWhen Reducing CO2 in an\nElectrochemical Flow Cell","volume":"5","author":"Zhang","year":"2020","journal-title":"ACS Energy Lett."},{"issue":"38","key":"2026102111101881600_cit6","doi-asserted-by":"publisher","first-page":"18986","DOI":"10.1021\/acs.jpcc.3c03563","article-title":"Interplay\nof Local pH and Cation Hydrolysis during Electrochemical CO2 Reduction\nVisualized by In Operando Chemical Shift-Resolved Magnetic Resonance\nImaging","volume":"127","author":"Schatz","year":"2023","journal-title":"J. Phys. Chem. C"},{"issue":"38","key":"2026102111101881600_cit7","doi-asserted-by":"publisher","first-page":"20896","DOI":"10.1021\/acs.jpcc.1c06265","article-title":"Operando Local pH\nMeasurement within Gas Diffusion Electrodes Performing Electrochemical\nCarbon Dioxide Reduction","volume":"125","author":"Welch","year":"2021","journal-title":"J. Phys. Chem. C"},{"issue":"4","key":"2026102111101881600_cit8","doi-asserted-by":"publisher","first-page":"1783","DOI":"10.1039\/D2EE02607D","article-title":"Direct Observation of the Local Microenvironment\nin Inhomogeneous CO2 Reduction Gas Diffusion Electrodes via Versatile\npOH Imaging","volume":"16","author":"Bo\u0308hme","year":"2023","journal-title":"Energy Environ. Sci."},{"issue":"10","key":"2026102111101881600_cit9","doi-asserted-by":"publisher","first-page":"7249","DOI":"10.1021\/acs.analchem.0c00844","article-title":"In Situ Fluorescence\nTomography Enables a 3D Mapping of Enzymatic O2 Reduction at the Electrochemical\nInterface","volume":"92","author":"Tassy","year":"2020","journal-title":"Anal. Chem."},{"issue":"45","key":"2026102111101881600_cit10","doi-asserted-by":"publisher","first-page":"15604","DOI":"10.1021\/acs.analchem.2c02135","article-title":"Local pH Modulation\nduring Electro-Enzymatic O2 Reduction:\nCharacterization of the Influence of Ionic Strength by in Situ Fluorescence\nMicroscopy","volume":"94","author":"Man","year":"2022","journal-title":"Anal. Chem."},{"issue":"19","key":"2026102111101881600_cit11","doi-asserted-by":"publisher","first-page":"6205","DOI":"10.1021\/ac050800y","article-title":"Fluorescence Confocal\nLaser Scanning Microscopy as\na Probe of pH Gradients in Electrode Reactions and Surface Activity","volume":"77","author":"Rudd","year":"2005","journal-title":"Anal. Chem."},{"issue":"17","key":"2026102111101881600_cit12","doi-asserted-by":"publisher","first-page":"7042","DOI":"10.1021\/acs.jpclett.0c01575","article-title":"Electrochemically Induced pH Change:\nTime-Resolved Confocal Fluorescence Microscopy Measurements and Comparison\nwith Numerical Model","volume":"11","author":"Pande","year":"2020","journal-title":"J. Phys. Chem. Lett."},{"issue":"1","key":"2026102111101881600_cit13","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/0022-0728(95)04236-7","article-title":"Theoretical Treatment of Diffusion and Kinetics in\nAmperometric Immobilized Enzyme Electrodes Part I: Redox Mediator\nEntrapped within the Film","volume":"397","author":"Bartlett","year":"1995","journal-title":"J. Electroanal. Chem."},{"issue":"1","key":"2026102111101881600_cit14","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1002\/fuce.200800028","article-title":"Modelling of Reaction and Diffusion Processes in a\nHigh-Surface-Area Biofuel Cell Electrode Made of Redox Polymer-Grafted\nCarbon","volume":"9","author":"Tamaki","year":"2009","journal-title":"Fuel Cells"},{"issue":"10","key":"2026102111101881600_cit15","doi-asserted-by":"publisher","first-page":"2145","DOI":"10.1016\/j.electacta.2004.09.022","article-title":"Oxygen Transport in Composite Mediated Biocathodes","volume":"50","author":"Calabrese Barton","year":"2005","journal-title":"Electrochim. Acta"},{"key":"2026102111101881600_cit16","doi-asserted-by":"publisher","first-page":"137483","DOI":"10.1016\/j.electacta.2020.137483","article-title":"Cyclic Voltammetry\nand Electrochemical\nImpedance Simulations of the Mediator-Type Enzyme Electrode Reaction\nUsing Finite Element Method","volume":"367","author":"Loew","year":"2021","journal-title":"Electrochim. Acta"},{"issue":"Pt A","key":"2026102111101881600_cit17","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.bioelechem.2015.07.007","article-title":"Dynamic and\nSteady State 1-D Model of Mediated Electron\nTransfer in a Porous Enzymatic Electrode","volume":"106","author":"Do","year":"2015","journal-title":"Bioelectrochemistry"},{"issue":"9","key":"2026102111101881600_cit18","doi-asserted-by":"publisher","first-page":"H671","DOI":"10.1149\/2.0711509jes","article-title":"Enzyme-Catalyzed Oxygen Reduction\nReaction in Biofuel Cells: Analytical Expressions for Chronoamperometric\nCurrent Densities","volume":"162","author":"Rasi","year":"2015","journal-title":"J. Electrochem. Soc."},{"issue":"3","key":"2026102111101881600_cit19","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1002\/fuce.201500025","article-title":"Theoretical Analysis of Reaction\nand Diffusion Processes in a Biofuel Cell Electrode","volume":"15","author":"Saravanakumar","year":"2015","journal-title":"Fuel Cells"},{"issue":"1","key":"2026102111101881600_cit20","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.coelec.2016.11.003","article-title":"Mathematical Modeling of Nonlinear\nReaction\u2013Diffusion Processes in Enzymatic Biofuel Cells","volume":"1","author":"Rajendran","year":"2017","journal-title":"Curr. Opin. Electrochem."},{"key":"2026102111101881600_cit21","doi-asserted-by":"publisher","first-page":"616","DOI":"10.1016\/j.electacta.2014.06.031","article-title":"Mathematical\nModeling of a Porous Enzymatic Electrode with Direct Electron Transfer\nMechanism","volume":"137","author":"Do","year":"2014","journal-title":"Electrochim. Acta"},{"key":"2026102111101881600_cit22","doi-asserted-by":"publisher","first-page":"117157","DOI":"10.1016\/j.ces.2021.117157","article-title":"Multiscale Modelling\nof Diffusion and Enzymatic Reaction in Porous\nElectrodes in Direct Electron Transfer Mode","volume":"248","author":"Le","year":"2022","journal-title":"Chem. Eng. Sci."},{"key":"2026102111101881600_cit23","doi-asserted-by":"publisher","first-page":"101655","DOI":"10.1016\/j.mex.2022.101655","article-title":"Numerical Tools for\nthe Simulation of Enzymatic Bio\nPorous-Electrodes Operating in DET Mode","volume":"9","author":"Le","year":"2022","journal-title":"MethodsX"},{"issue":"9","key":"2026102111101881600_cit24","doi-asserted-by":"publisher","first-page":"1966","DOI":"10.1039\/C7EE01830D","article-title":"Impact of Substrate\nDiffusion and Enzyme Distribution in 3D-Porous Electrodes: A Combined\nElectrochemical and Modelling Study of a Thermostable H2\/O2 Enzymatic\nFuel Cell","volume":"10","author":"Mazurenko","year":"2017","journal-title":"Energy Environ. Sci."},{"issue":"7","key":"2026102111101881600_cit25","doi-asserted-by":"publisher","first-page":"4694","DOI":"10.3390\/en7074694","article-title":"Modeling and\nSimulation of Enzymatic\nBiofuel Cells with Three-Dimensional Microelectrodes","volume":"7","author":"Song","year":"2014","journal-title":"Energies"},{"key":"2026102111101881600_cit26","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1016\/j.electacta.2013.08.044","article-title":"Mathematical Modelling\nof an Enzymatic Fuel Cell with an Air-Breathing Cathode","volume":"112","author":"Osman","year":"2013","journal-title":"Electrochim. Acta"},{"issue":"4","key":"2026102111101881600_cit27","doi-asserted-by":"publisher","first-page":"e2114097119","DOI":"10.1073\/pnas.2114097119","article-title":"Understanding the Local Chemical\nEnvironment of Bioelectrocatalysis","volume":"119","author":"Edwardes Moore","year":"2022","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"30","key":"2026102111101881600_cit28","doi-asserted-by":"publisher","first-page":"3921","DOI":"10.1039\/b800799c","article-title":"O2 Reduction to H2O by the Multicopper\nOxidases","author":"Solomon","year":"2008","journal-title":"Dalton Trans."},{"issue":"51","key":"2026102111101881600_cit29","doi-asserted-by":"publisher","first-page":"17788","DOI":"10.1021\/ja509150j","article-title":"Mechanism of the Reduction of the\nNative Intermediate in the Multicopper Oxidases: Insights into Rapid\nIntramolecular Electron Transfer in Turnover","volume":"136","author":"Heppner","year":"2014","journal-title":"J. Am. Chem. Soc."},{"issue":"6","key":"2026102111101881600_cit30","doi-asserted-by":"publisher","first-page":"3916","DOI":"10.1021\/acscatal.7b01286","article-title":"Mechanism of Chloride\nInhibition of Bilirubin Oxidases and Its Dependence on Potential and\npH","volume":"7","author":"de Poulpiquet","year":"2017","journal-title":"ACS Catal."},{"issue":"28","key":"2026102111101881600_cit31","doi-asserted-by":"publisher","first-page":"11304","DOI":"10.1021\/jacs.9b05230","article-title":"O2 Reduction to Water\nby High Potential Multicopper Oxidases: Contributions of the T1 Copper\nSite Potential and the Local Environment of the Trinuclear Copper\nCluster","volume":"141","author":"Sekretaryova","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"5","key":"2026102111101881600_cit32","doi-asserted-by":"publisher","first-page":"2392","DOI":"10.1021\/acs.chemrev.7b00220","article-title":"O2 Reduction\nin Enzymatic Biofuel Cells","volume":"118","author":"Mano","year":"2018","journal-title":"Chem. Rev."},{"issue":"6","key":"2026102111101881600_cit33","doi-asserted-by":"publisher","first-page":"437","DOI":"10.5796\/electrochemistry.72.437","article-title":"Kinetic Study of Direct\nBioelectrocatalysis of Dioxygen Reduction with Bilirubin Oxidase at\nCarbon Electrodes","volume":"72","author":"Tsujimura","year":"2004","journal-title":"Electrochemistry"},{"issue":"39","key":"2026102111101881600_cit34","doi-asserted-by":"publisher","first-page":"13882","DOI":"10.1021\/ja5077519","article-title":"Modeling\nDioxygen Reduction at Multicopper\nOxidase Cathodes","volume":"136","author":"Agbo","year":"2014","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026102111101881600_cit35","doi-asserted-by":"publisher","first-page":"1232","DOI":"10.1021\/jp2086285","article-title":"Voltammetry and Single-Molecule in\nSitu Scanning Tunneling\nMicroscopy of Laccases and Bilirubin Oxidase in Electrocatalytic Dioxygen\nReduction on Au(111) Single-Crystal Electrodes","volume":"116","author":"Climent","year":"2012","journal-title":"J. Phys. Chem. C"},{"issue":"5","key":"2026102111101881600_cit36","doi-asserted-by":"publisher","first-page":"1567","DOI":"10.1039\/c2sc00632d","article-title":"Developing the Mechanism\nof Dioxygen Reduction Catalyzed\nby Multicopper Oxidases Using Protein Film Electrochemistry","volume":"3","author":"Cracknell","year":"2012","journal-title":"Chem. Sci."},{"key":"2026102111101881600_cit37","article-title":"Fundamentals of Enzyme Kinetics","volume-title":"Completely Revised and Greatly Enlarged ed","author":"Cornish-Bowden","year":"2012","edition":"4"},{"key":"2026102111101881600_cit38","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-7091-1402-5","volume-title":"Kinetics of Enzyme-Modifier\nInteractions: Selected Topics in the Theory and Diagnosis of Inhibition\nand Activation Mechanisms","author":"Baici","year":"2015"},{"issue":"50","key":"2026102111101881600_cit39","doi-asserted-by":"publisher","first-page":"13058","DOI":"10.1021\/jp0265687","article-title":"Effect\nof a Dispersion of Interfacial Electron Transfer Rates on Steady State\nCatalytic Electron Transport in [NiFe]-Hydrogenase and Other Enzymes","volume":"106","author":"Le\u0301ger","year":"2002","journal-title":"J. Phys. Chem. B"},{"issue":"1","key":"2026102111101881600_cit40","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.coelec.2016.11.002","article-title":"Modelling\nthe Voltammetry of Adsorbed Enzymes and Molecular\nCatalysts","volume":"1","author":"Fourmond","year":"2017","journal-title":"Curr. Opin. Electrochem."},{"key":"2026102111101881600_cit41","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.bioelechem.2013.11.007","article-title":"The pH Dependence of\nthe Cathodic Peak Potential of the Active Sites\nin Bilirubin Oxidase","volume":"96","author":"Filip","year":"2014","journal-title":"Bioelectrochemistry"},{"issue":"7","key":"2026102111101881600_cit42","doi-asserted-by":"publisher","first-page":"1524","DOI":"10.1002\/elan.201200188","article-title":"On the Possibility\nof Uphill Intramolecular Electron Transfer in Multicopper Oxidases:\nElectrochemical and Quantum Chemical Study of Bilirubin Oxidase","volume":"24","author":"Shleev","year":"2012","journal-title":"Electroanalysis"},{"issue":"22","key":"2026102111101881600_cit43","doi-asserted-by":"publisher","first-page":"8742","DOI":"10.1039\/C6TA02654K","article-title":"Direct Electron Transfer-Type\nDual\nGas Diffusion H 2\/O 2 Biofuel Cells","volume":"4","author":"So","year":"2016","journal-title":"J. Mater.\nChem. A"},{"key":"2026102111101881600_cit44","doi-asserted-by":"publisher","first-page":"794","DOI":"10.1016\/j.electacta.2017.06.117","article-title":"Highly Permeable Gas Diffusion Electrodes\nwith Hollow Carbon Nanotubes for Bilirubin Oxidase-Catalyzed Dioxygen\nReduction","volume":"246","author":"So","year":"2017","journal-title":"Electrochim. Acta"},{"issue":"35","key":"2026102111101881600_cit45","doi-asserted-by":"publisher","first-page":"23074","DOI":"10.1021\/acsami.6b07355","article-title":"How the Intricate\nInteractions\nbetween Carbon Nanotubes and Two Bilirubin Oxidases Control Direct\nand Mediated O2 Reduction","volume":"8","author":"Mazurenko","year":"2016","journal-title":"ACS Appl.\nMater. Interfaces"},{"issue":"42","key":"2026102111101881600_cit46","doi-asserted-by":"publisher","first-page":"13962","DOI":"10.1039\/c0cp00018c","article-title":"Mechanistic\nStudies of the \u2018Blue\u2019 Cu Enzyme, Bilirubin Oxidase,\nas a Highly Efficient Electrocatalyst for the Oxygen Reduction Reaction","volume":"12","author":"Dos Santos","year":"2010","journal-title":"Phys. Chem. Chem. Phys."},{"key":"2026102111101881600_cit47","doi-asserted-by":"publisher","first-page":"1059","DOI":"10.1016\/j.electacta.2017.03.114","article-title":"Reliable Estimation\nof the Kinetic Parameters of Redox Enzymes by Taking into Account\nMass Transport towards Rotating Electrodes in Protein Film Voltammetry\nExperiments","volume":"245","author":"Merrouch","year":"2017","journal-title":"Electrochim. Acta"},{"issue":"3","key":"2026102111101881600_cit48","doi-asserted-by":"publisher","first-page":"1394","DOI":"10.1021\/jp054783s","article-title":"Interpreting the Catalytic\nVoltammetry of an Adsorbed Enzyme by Considering\nSubstrate Mass Transfer, Enzyme Turnover, and Interfacial Electron\nTransport","volume":"110","author":"Reda","year":"2006","journal-title":"J. Phys. Chem. B"},{"issue":"1","key":"2026102111101881600_cit49","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1042\/bj0550161","article-title":"The Effect\nof pH on the Affinities of Enzymes for Substrates and Inhibitors","volume":"55","author":"Dixon","year":"1953","journal-title":"Biochem. 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Understanding Natural Convection","volume":"87","author":"Ngamchuea","year":"2015","journal-title":"Anal. Chem."},{"issue":"1\u20132","key":"2026102111101881600_cit53","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/S0022-0728(00)00378-8","article-title":"The Real Meaning\nof Nernst\u2019s Steady Diffusion Layer Concept under Non-Forced\nHydrodynamic Conditions. A Simple Model Based on Levich\u2019s Seminal\nView of Convection","volume":"500","author":"Amatore","year":"2001","journal-title":"J. Electroanal. 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