{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T16:12:11Z","timestamp":1779379931490,"version":"3.53.1"},"reference-count":98,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2024,11,20]],"date-time":"2024-11-20T00:00:00Z","timestamp":1732060800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Simons Foundation award","award":["1030281"],"award-info":[{"award-number":["1030281"]}]},{"name":"Simons Foundation award","award":["2021.01\/0010"],"award-info":[{"award-number":["2021.01\/0010"]}]},{"name":"Simons Foundation award","award":["STCU 7113"],"award-info":[{"award-number":["STCU 7113"]}]},{"name":"NRF grant of Ukraine","award":["1030281"],"award-info":[{"award-number":["1030281"]}]},{"name":"NRF grant of Ukraine","award":["2021.01\/0010"],"award-info":[{"award-number":["2021.01\/0010"]}]},{"name":"NRF grant of Ukraine","award":["STCU 7113"],"award-info":[{"award-number":["STCU 7113"]}]},{"name":"US NSF grant CBET-2235349","award":["1030281"],"award-info":[{"award-number":["1030281"]}]},{"name":"US NSF grant CBET-2235349","award":["2021.01\/0010"],"award-info":[{"award-number":["2021.01\/0010"]}]},{"name":"US NSF grant CBET-2235349","award":["STCU 7113"],"award-info":[{"award-number":["STCU 7113"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biosensors"],"abstract":"<jats:p>We report the development of amperometric biosensors (ABSs) employing flavocytochrome b2 (Fcb2) coupled with nanoparticles (NPs) of noble metals on graphite electrode (GE) surfaces. Each NPs\/GE configuration was evaluated for its ability to decompose hydrogen peroxide (H2O2), mimicking peroxidase (PO) activity. The most effective nanoPO (nPO) was selected for developing ABSs targeting L-lactate. Consequently, several Fcb2\/nPO-based ABSs with enhanced sensitivity to L-lactate were developed, demonstrating mediated ET between Fcb2 and the GE surface. The positive effect of noble metal NPs on Fcb2-based sensor sensitivity may be explained by the synergy between their dual roles as both PO mimetics and electron transfer mediators. Furthermore, our findings provide preliminary data that may prompt a re-evaluation of the mechanism of L-lactate oxidation in Fcb2-mediated catalysis. Previously, it was believed that L-lactate oxidation via Fcb2 catalysis did not produce H2O2, unlike catalysis via L-lactate oxidase. Our initial research revealed that the inclusion of nPO in Fcb2-based ABSs significantly increased their sensitivity. Employing other PO mimetics in ABSs for L-lactate yielded similar results, reinforcing our hypothesis that trace amounts of H2O2 may be generated as a transient intermediate in this reaction. The presence of nPO enhances the L-lactate oxidation rate through H2O2 utilization, leading to signal amplification and heightened bioelectrode sensitivity. The proposed ABSs have been successfully tested on blood serum and fermented food samples, showing their promise for L-lactate monitoring in medicine and the food industry.<\/jats:p>","DOI":"10.3390\/bios14110562","type":"journal-article","created":{"date-parts":[[2024,11,20]],"date-time":"2024-11-20T07:02:58Z","timestamp":1732086178000},"page":"562","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Peroxidase-like Nanoparticles of Noble Metals Stimulate Increasing Sensitivity of Flavocytochrome b2-Based L-Lactate Biosensors"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4015-8083","authenticated-orcid":false,"given":"Galina","family":"Gayda","sequence":"first","affiliation":[{"name":"Department of Analytical Biotechnology, Institute of Cell Biology National Academy of Sciences of Ukraine, 14\/16 Drahomanov Str., 79005 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olha","family":"Demkiv","sequence":"additional","affiliation":[{"name":"Department of Analytical Biotechnology, Institute of Cell Biology National Academy of Sciences of Ukraine, 14\/16 Drahomanov Str., 79005 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nataliya","family":"Stasyuk","sequence":"additional","affiliation":[{"name":"Department of Analytical Biotechnology, Institute of Cell Biology National Academy of Sciences of Ukraine, 14\/16 Drahomanov Str., 79005 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuriy","family":"Boretsky","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Hygiene, Ivan Boberskyi Lviv State University of Physical Culture, 11 Kostiushko Str., 79000 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8861-4477","authenticated-orcid":false,"given":"Mykhailo","family":"Gonchar","sequence":"additional","affiliation":[{"name":"Department of Analytical Biotechnology, Institute of Cell Biology National Academy of Sciences of Ukraine, 14\/16 Drahomanov Str., 79005 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8493-713X","authenticated-orcid":false,"given":"Marina","family":"Nisnevitch","sequence":"additional","affiliation":[{"name":"Department of Chemical Engineering, Ariel University, Kyriat-ha-Mada, Ariel 4070000, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Guzm\u00e1n, J.J., Sierra-Padilla, A., Palacios-Santander, J.M., Fern\u00e1ndez-Alba, J.J., Mac\u00edas, C.G., and Cubillana-Aguilera, L. (2022). What is left for real-life lactate monitoring? Current advances in electrochemical lactate (bio)sensors for agrifood and biomedical applications. Biosensors, 12.","DOI":"10.3390\/bios12110919"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Wijayanti, S.D., Tsvik, L., and Haltrich, D. (2023). Recent advances in electrochemical enzyme-based biosensors for food and beverage analysis. Foods, 12.","DOI":"10.3390\/foods12183355"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Smutok, O., Dmytruk, K., Kavetskyy, T., Sibirny, A., and Gonchar, M. (2021). Flavocytochrome b2 of the Methylotrophic Yeast Ogataea polymorpha: Construction of Overproducers, Purification, and Bioanalytical Application. Flavin and Flavoproteins: Methods Molecular Biology, Springer.","DOI":"10.1007\/978-1-0716-1286-6_16"},{"key":"ref_4","first-page":"119","article-title":"Effective Technologies for Isolating Yeast Oxido-Reductases of Analytical Importance","volume":"Volume 5","author":"Andriy","year":"2019","journal-title":"Non-Conventional Yeasts: From Basic Research to Application"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1007\/s10311-020-01106-6","article-title":"Lactate detection sensors for food, clinical and biological applications: A review","volume":"19","author":"Rattu","year":"2021","journal-title":"Environ. Chem. Lett."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1097\/ALN.0000000000003904","article-title":"Clinical use of lactate measurements: Comment","volume":"135","author":"Bahlmann","year":"2021","journal-title":"Anesthesiology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1007\/s00134-007-0679-y","article-title":"Don\u2019t take vitals, take a lactate","volume":"33","author":"Bakker","year":"2007","journal-title":"Intensive Care Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s12276-022-00802-3","article-title":"Tracing the lactate shuttle to the mitochondrial reticulum","volume":"54","author":"Brooks","year":"2022","journal-title":"Exp. Mol. Med."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1007\/s10877-021-00685-1","article-title":"Clinical evaluation of a novel subcutaneous lactate monitor","volume":"36","author":"Dror","year":"2022","journal-title":"J. Clin. Monit. Comput."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Crapnell, R.D., Tridente, A., Banks, C.E., and Dempsey-Hibbert, N.C. (2021). Evaluating the possibility of translating technological advances in non-invasive continuous lactate monitoring into critical care. Sensors, 21.","DOI":"10.3390\/s21030879"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1097\/CNQ.0000000000000311","article-title":"Continuous lactate measurement devices and implications for critical care: A literature review","volume":"43","author":"Chavez","year":"2020","journal-title":"Crit. Care Nurs. Q."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Frisardi, V., Canovi, S., Vaccaro, S., and Frazzi, R. (2023). The significance of microenvironmental and circulating lactate in breast cancer. Review. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242015369"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1007\/s00134-018-5213-x","article-title":"The ten pitfalls of lactate clearance in sepsis","volume":"45","author":"Hernandez","year":"2019","journal-title":"Intensive Care Med."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Kobayashi, Y., Peng, Y.C., Yu, E., Bush, B., Jung, Y.H., Murphy, Z., Goeddel, L., Whitman, G., Venkataraman, A., and Brown, C.H. (2023). Prediction of lactate concentrations after cardiac surgery using machine learning and deep learning approaches. Front. Med., 10.","DOI":"10.3389\/fmed.2023.1165912"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Meng, X., Wu, W., Tang, Y., Peng, M., Yang, J., Yuan, S., Hu, Z., and Liu, W. (2024). Lactate\/Hydroxycarboxylic acid receptor 1 in Alzheimer\u2019s disease: Mechanisms and therapeutic implications-exercise perspective. Mol. Neurobiol., 61.","DOI":"10.1007\/s12035-024-04067-x"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Li, S., Li, H., Lu, Y., Zhou, M., Jiang, S., Du, X., and Guo, C. (2023). Advanced Textile-Based Wearable Biosensors for Healthcare Monitoring. Biosensors, 13.","DOI":"10.3390\/bios13100909"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e24719","DOI":"10.1016\/j.heliyon.2024.e24719","article-title":"Chronic lactate exposure promotes cardiomyocyte cytoskeleton remodelling","volume":"10","author":"Luti","year":"2024","journal-title":"Heliyon"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e24421","DOI":"10.1016\/j.heliyon.2024.e24421","article-title":"The effects of long-term lactate and high-intensity interval training (HIIT) on brain neuroplasticity of aged mice","volume":"10","author":"Lei","year":"2024","journal-title":"Heliyon"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"e1614","DOI":"10.1002\/ctm2.1614","article-title":"Histone lactylation bridges metabolic reprogramming and epigenetic rewiring in driving carcinogenesis: Oncometabolite fuels oncogenic transcription","volume":"14","author":"Zhang","year":"2024","journal-title":"Clin. Transl. Med."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1017\/S1049023X23006623","article-title":"The effectiveness of prehospital subcutaneous continuous lactate monitoring in adult trauma: A systematic review","volume":"39","author":"Scriven","year":"2024","journal-title":"Prehosp. Disaster Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1097\/ALN.0000000000003655","article-title":"Appropriate clinical use of lactate measurements","volume":"134","author":"Pino","year":"2021","journal-title":"Anesthesiology"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Wang, J., Wang, Z., Wang, Q., Li, X., and Guo, Y. (2024). Ubiquitous protein lactylation in health and diseases. Cell. Mol. Biol. Lett., 29.","DOI":"10.1186\/s11658-024-00541-5"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.7150\/ijbs.91492","article-title":"Histone lactylation: From tumor lactate metabolism to epigenetic regulation","volume":"20","author":"Yu","year":"2024","journal-title":"Int. J. Biol. Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1038\/s41420-024-01898-4","article-title":"Histone lactylation promotes malignant progression by facilitating USP39 expression to target PI3K\/AKT\/HIF-1\u03b1 signal pathway in endometrial carcinoma","volume":"10","author":"Wei","year":"2024","journal-title":"Cell Death Discov."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1021\/acscentsci.3c01250","article-title":"High-Performance Genetically Encoded Green Fluorescent Biosensors for Intracellular L-lactate","volume":"10","author":"Hario","year":"2024","journal-title":"ACS Cent. Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.cll.2015.05.006","article-title":"Use of lactate in small animal clinical practice. Review","volume":"35","author":"Sharkey","year":"2015","journal-title":"Clin. Lab. Med."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Xiao, D., Hu, C., Xu, X., L\u00fc, C., Wang, Q., Zhang, W., Gao, C., Xu, P., Wang, X., and Ma, C. (2022). A D,L-lactate biosensor based on allosteric transcription factor LldR and amplified luminescent proximity homogeneous assay. Biosens. Bioelectron., 211.","DOI":"10.1016\/j.bios.2022.114378"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1021\/acssensors.3c00708","article-title":"Fully integrated wearable device for continuous sweat lactate monitoring in sports","volume":"8","author":"Xuan","year":"2023","journal-title":"ACS Sens."},{"key":"ref_29","first-page":"3087","article-title":"A bifunctional wearable sensor based on a nanoporous membrane for simultaneous detection of sweat lactate and temperature","volume":"96","author":"Wu","year":"2024","journal-title":"Anal. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1002\/elps.202300179","article-title":"Capillary electrophoresis with capacitively coupled contactless conductivity detection (C4 D) for rapid and simple determination of lactate in sweat","volume":"45","author":"Rocha","year":"2024","journal-title":"Electrophoresis"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3496","DOI":"10.1021\/acssensors.1c01403","article-title":"Can wearable sweat lactate sensors contribute to sports physiology?","volume":"6","author":"Xuan","year":"2021","journal-title":"ACS Sens."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1249\/mss.0b013e318047ba.30","article-title":"The lactate paradox: Does acclimatization to high altitude affect blood lactate during exercise?","volume":"39","author":"Wagner","year":"2007","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.aej.2024.01.017","article-title":"Application of graphene oxide nanosheet lactate biosensors in continuous assessment of athlete fitness","volume":"88","author":"Deng","year":"2024","journal-title":"Alex. Eng. J."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Kub\u00e1\u0148, P., Dosed\u011blov\u00e1, V., Martma, K., Rannama, I., Reinpold, K., and Shimmo, R. (2021). Sub-minute analysis of lactate from a single blood drop using capillary electrophoresis with contactless conductivity detection in monitoring of athlete performance. Molecules, 26.","DOI":"10.3390\/molecules26195817"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"101420","DOI":"10.1016\/j.coelec.2023.101420","article-title":"Recent advances on nanomaterial-modified film-electrode-based sensors: Approach to clinical purpose","volume":"42","author":"Jampasa","year":"2023","journal-title":"Curr. Opin. Electrochem."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Yang, S., Tang, Z., Tian, Y., Ji, X., Wang, F., Xie, C., and He, Z. (2022). Dual-color fluorescent hydrogel microspheres combined with smartphones for visual detection of lactate. Biosensors, 12.","DOI":"10.3390\/bios12100802"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Kannan, P., and Maduraiveeran, G. (2023). Metal Oxides nanomaterials and nanocomposite-based electrochemical sensors for healthcare applications. Biosensors, 13.","DOI":"10.3390\/bios13050542"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"29584","DOI":"10.1039\/D3RA06108F","article-title":"Construction of the lactate-sensing fibremats by confining sensor fluorescent protein of lactate inside nanofibers of the poly(HPMA\/DAMA)\/ADH-nylon 6 core-shell fibremat","volume":"13","author":"Kato","year":"2023","journal-title":"RSC Adv."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"8732","DOI":"10.1021\/acsomega.2c08127","article-title":"Fabrication of a lactate-specific molecularly imprinted polymer toward disease detection","volume":"8","author":"Mustafa","year":"2023","journal-title":"ACS Omega"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Nien, Y.-H., Kang, Z.-X., Su, T.-Y., Ho, C.-S., Chou, J.-C., Lai, C.-H., Kuo, P.-Y., Lai, T.-Y., Dong, Z.-X., and Chen, Y.-Y. (2021). Investigation of flexible arrayed lactate biosensor based on copper doped zinc oxide films modified by iron\u2013platinum nanoparticles. Polymers, 13.","DOI":"10.3390\/polym13132062"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/j.bios.2016.07.076","article-title":"Determination of lactic acid with special emphasis on biosensing methods: A review","volume":"86","author":"Pundir","year":"2016","journal-title":"Biosens. Bioelectron."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s00216-013-7307-1","article-title":"Lactate biosensors: Current status and outlook","volume":"406","author":"Rassaei","year":"2014","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Boyarski, A., Shlush, N., Paz, S., Eichler, J., and Alfonta, L. (2023). Electrochemical characterization of a dual cytochrome-containing lactate dehydrogenase. Bioelectrochemistry, 152.","DOI":"10.1016\/j.bioelechem.2023.108406"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Cohen, R., Herzallh, N.S., Meirovich, M.M., Bachar, O., Frech, L., Cohen, Y., and Yehezkeli, O. (2023). An Oxygen-Insensitive biosensor and a biofuel cell device based on FMN L-lactate dehydrogenase. Bioelectrochemistry, 149.","DOI":"10.1016\/j.bioelechem.2022.108316"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Demkiv, O., Gayda, G., Stasyuk, N., Moroz, A., Serkiz, R., Kausaite-Minkstimiene, A., Gonchar, M., and Nisnevitch, M. (2023). Flavocytochrome b2-mediated electroactive nanoparticles for developing amperometric L-lactate biosensors. Biosensors, 13.","DOI":"10.3390\/bios13060587"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Thongkhao, P., Numnuam, A., Khongkow, P., Sangkhathat, S., and Phairatana, T. (2024). Disposable polyaniline\/m-phenylenediamine-based electrochemical lactate biosensor for early sepsis diagnosis. Polymers, 16.","DOI":"10.3390\/polym16040473"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"41480","DOI":"10.1021\/acsomega.2c05257","article-title":"Flavin mononucleotide-dependent L-lactate dehydrogenases: Expanding the toolbox of enzymes for L-lactate biosensors","volume":"7","author":"Tsvik","year":"2022","journal-title":"ACS Omega"},{"key":"ref_48","unstructured":"(2024, October 18). BRENDA Enzyme Database. Available online: https:\/\/www.brenda-enzymes.org\/all_enzymes.php."},{"key":"ref_49","first-page":"153","article-title":"Flavocytochrome b2","volume":"Volume II","year":"1991","journal-title":"Chemistry and Biochemistry of Flavoenzymes"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1002\/2211-5463.13534","article-title":"Further evidence in favour of a carbanion mechanism for glycolate oxidase","volume":"13","author":"Pasquier","year":"2023","journal-title":"FEBS Open Bio"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1007\/0-306-46828-X_8","article-title":"Flavocytochrome b2","volume":"Volume 35","author":"Holzenburg","year":"2000","journal-title":"Enzyme-Catalyzed Electron and Radical Transfer. Subcellular Biochemistry"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"13080","DOI":"10.1021\/bi7013757","article-title":"Flavocytochrome b2: Reactivity of its flavin with molecular oxygen","volume":"46","author":"Boubacar","year":"2007","journal-title":"Biochemistry"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"8932","DOI":"10.1021\/bi962425x","article-title":"Resonance Raman study on the oxidized and anionic semiquinone forms of flavocytochrome b2 and L-lactate monooxygenase. Influence of the structure and environment of the isoalloxazine ring on the flavin function","volume":"36","author":"Tegoni","year":"1997","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"6345","DOI":"10.1021\/bi9522559","article-title":"New insights into the catalytic cycle of flavocytochrome b2","volume":"35","author":"Daff","year":"1996","journal-title":"Biochemistry"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1042\/bj2630973","article-title":"Structural basis for the kinetic differences between flavocytochromes b2 from the yeasts Hansenula anomala and Saccharomyces cerevisiae","volume":"263","author":"Black","year":"1989","journal-title":"Biochem. J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.abb.2009.10.005","article-title":"Flavin-containing heme enzymes","volume":"493","author":"Mowat","year":"2010","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/0300-9084(96)88168-5","article-title":"Flavocytochrome b2-cytochrome c interactions: The electron transfer reaction revisited","volume":"77","year":"1995","journal-title":"Biochimie"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1007\/s00249-011-0697-0","article-title":"Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b2","volume":"40","author":"Lederer","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4661","DOI":"10.1021\/bi602634y","article-title":"Potentiometric and further kinetic characterization of the flavin-binding domain of Saccharomyces cerevisiae flavocytochrome b2. Inhibition by anions binding in the active site","volume":"46","author":"Terrier","year":"2007","journal-title":"Biochemistry"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1042\/bj2910089","article-title":"The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b2","volume":"291","author":"White","year":"1993","journal-title":"Biochem. J."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1111\/j.1432-1033.1980.tb04450.x","article-title":"Flavocytochrome b2 (baker\u2018s yeast). Deuterium isotope effect studied by rapid-kinetic methods as a probe for the mechanism of electron transfer","volume":"104","author":"Pompon","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"15208","DOI":"10.1021\/bi035546n","article-title":"Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism","volume":"42","author":"Sobrado","year":"2003","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"9519","DOI":"10.1021\/bi049263m","article-title":"Altered substrate specificity in flavocytochrome b2: Structural insights into the mechanism of L-lactate dehydrogenation","volume":"43","author":"Mowat","year":"2004","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.bioorg.2003.02.001","article-title":"Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations","volume":"32","author":"Fitzpatrick","year":"2004","journal-title":"Bioorg. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2368","DOI":"10.1111\/j.1742-4658.2009.06969.x","article-title":"L-lactate dehydrogenation in flavocytochrome b2","volume":"276","author":"Tabacchi","year":"2009","journal-title":"FEBS J."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1016\/j.bbapap.2016.05.001","article-title":"Trifluorosubstrates as mechanistic probes for an FMN-dependent l-2-hydroxy acid-oxidizing enzyme","volume":"1864","author":"Lederer","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/BF00254891","article-title":"An EPR study of the interactions between heme and flavin in yeast flavocytochrome b2","volume":"14","author":"Bertrand","year":"1987","journal-title":"Eur. Biophys. J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1042\/bj3330107","article-title":"L-Mandelate dehydrogenase from Rhodotorula graminis: Cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain","volume":"333","author":"Illias","year":"1998","journal-title":"Biochem. J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.bbapap.2016.12.007","article-title":"Translational misreading, amino acid misincorporation and misinterpretations. The case of the flavocytochrome b2 H373Q variant","volume":"1865","author":"Machillot","year":"2017","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1042\/bj2950501","article-title":"Expression in Escherichia coli of the flavin and the haem domains of Hansenula anomala flavocytochrome b2 (flavodehydrogenase and b2 core) and characterization of the recombinant proteins","volume":"295","author":"Silvestrini","year":"1993","journal-title":"Biochem. J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2874","DOI":"10.1073\/pnas.0806798106","article-title":"Genomic reconstruction of Shewanella oneidensis MR-1 metabolism reveals a previously uncharacterized machinery for lactate utilization","volume":"106","author":"Pinchuk","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1021\/acsmeasuresciau.1c00038","article-title":"Use of protein engineering to elucidate electron transfer pathways between proteins and electrodes","volume":"2","author":"Algov","year":"2021","journal-title":"ACS Meas. Sci. Au"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1016\/0022-2836(90)90240-M","article-title":"Molecular structure of flavocytochrome b2 at 2.4 A resolution","volume":"212","author":"Xia","year":"1990","journal-title":"J. Mol. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"11376","DOI":"10.1021\/bi00161a015","article-title":"Mutation of the heme-binding crevice of flavocytochrome b2 from Saccharomyces cerevisiae: Altered heme potential and absence of redox cooperativity between heme and FMN centers","volume":"31","author":"Kay","year":"1992","journal-title":"Biochemistry"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Schachinger, F., Chang, H., Scheiblbrandner, S., and Ludwig, R. (2021). Amperometric biosensors based on direct electron transfer enzymes. Molecules, 26.","DOI":"10.3390\/molecules26154525"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"15609","DOI":"10.1039\/C6CP00395H","article-title":"QM\/MM study of l-lactate oxidation by flavocytochrome b2","volume":"18","author":"Gillet","year":"2016","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1021\/acs.chemrev.7b00650","article-title":"same substrate, many reactions: Oxygen activation in flavoenzymes","volume":"118","author":"Romero","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1002\/celc.201801256","article-title":"Direct electron transfer of enzymes facilitated by cytochromes","volume":"6","author":"Ma","year":"2019","journal-title":"ChemElectroChem"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Matysik, J., Gerhards, L., Theiss, T., Timmermann, L., Kurle-Tucholski, P., Musabirova, G., Qin, R., Ortmann, F., Solov\u2019yov, I.A., and Gulder, T. (2023). Spin dynamics of flavoproteins. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24098218"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Stasyuk, N., Gayda, G., Demkiv, O., Darmohray, L., Gonchar, M., and Nisnevitch, M. (2021). Amperometric biosensors for L-arginine determination based on L-arginine oxidase and peroxidase-like nanozymes. Appl. Sci., 11.","DOI":"10.3390\/app11157024"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1007\/s00604-023-05753-8","article-title":"Nanozyme can substitute a natural Ogataea polymorpha catalase enzyme in vivo","volume":"190","author":"Prokopiv","year":"2023","journal-title":"Mikrochim. Acta"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Demkiv, O., Gayda, G., Stasyuk, N., Brahinetz, O., Gonchar, M., and Nisnevitch, M. (2022). Nanomaterials as redox mediators in laccase-based amperometric biosensors for catechol assay. Biosensors, 12.","DOI":"10.3390\/bios12090741"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Hou, L., Jiang, G., Sun, Y., Zhang, X., Huang, J., Liu, S., Lin, T., Ye, F., and Zhao, S. (2019). Progress and Trend on the Regulation Methods for Nanozyme Activity and Its Application. Catalysts, 9.","DOI":"10.3390\/catal9121057"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.actbio.2021.02.036","article-title":"Chemical design of nanozymes for biomedical applications","volume":"126","author":"Wei","year":"2021","journal-title":"Acta Biomater."},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Demkiv, O., Stasyuk, N., Serkiz, R., Gayda, G., Nisnevitch, M., and Gonchar, M. (2021). Peroxidase-Like Metal-Based Nanozymes: Synthesis, Catalytic Properties, and Analytical Application. Appl. Sci., 11.","DOI":"10.3390\/app11020777"},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Gayda, G.Z., Demkiv, O.M., Gurianov, Y., Serkiz, R.Y., Klepach, H.M., Gonchar, M.V., and Nisnevitch, M. (2021). \u201cGreen\u201d Prussian blue analogues as peroxidase mimetics for amperometric sensing and biosensing. Biosensors, 11.","DOI":"10.3390\/bios11060193"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1007\/s00604-024-06319-y","article-title":"Correction: Ammonium nanochelators in conjunction with arginine-specific enzymes in amperometric biosensors for arginine assay","volume":"191","author":"Stasyuk","year":"2024","journal-title":"Microchim. Acta"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Stasyuk, N., Demkiv, O., Gayda, G., Zakalskiy, A., Klepach, H., Bisko, N., Gonchar, M., and Nisnevitch, M. (2022). Highly Porous 3D Gold Enhances Sensitivity of Amperometric Biosensors Based on Oxidases and CuCe Nanoparticles. Biosensors, 12.","DOI":"10.3390\/bios12070472"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Stasyuk, N., Smutok, O., Demkiv, O., Prokopiv, T., Gayda, G., Nisnevitch, M., and Gonchar, M. (2020). Synthesis, Catalytic Properties and Application in Biosensorics of Nanozymes and Electronanocatalysts: A Review. Sensors, 20.","DOI":"10.3390\/s20164509"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Yang, G., Hong, J., and Park, S.B. (2024). Wearable device for continuous sweat lactate monitoring in sports: A narrative review. Front. Physiol., 15.","DOI":"10.3389\/fphys.2024.1376801"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"4819","DOI":"10.1080\/10408398.2021.2007844","article-title":"Impact of lactic acid bacteria and their metabolites on the techno-functional properties and health benefits of fermented dairy products","volume":"63","author":"Sharma","year":"2021","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1128\/aem.60.7.2627-2636.1994","article-title":"Kinetics and modeling of lactic acid production by Lacto-bacillus plantarum","volume":"60","author":"Passos","year":"1994","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"114574","DOI":"10.1016\/j.lwt.2023.114574","article-title":"Non-aminobiogenic starter cultures in a model system of cucumber fermentation","volume":"177","author":"Roszko","year":"2023","journal-title":"LWT"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1111\/1750-3841.15990","article-title":"Changes in the free amino acid profile of pickling cucumber during lactic acid fermentation","volume":"87","author":"Moore","year":"2022","journal-title":"Food Sci."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/j.bios.2004.04.020","article-title":"A novel L-lactate-selective biosensor based on the use of flavocyto-chrome b2 from methylotrophic yeast Hansenula polymorpha","volume":"20","author":"Smutok","year":"2005","journal-title":"Biosens. Bioelectron."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0531-5131(02)00519-8","article-title":"The reactivity of oxygen with flavoproteins","volume":"1233","author":"Massey","year":"2002","journal-title":"Int. Congr. Ser."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.tibs.2006.03.003","article-title":"To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes","volume":"31","author":"Mattevi","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1016\/j.electacta.2007.02.028","article-title":"Localised visualisation of O2 consumption and H2O2 formation by means of SCM for the characterisation of fuel cell catalyst activity","volume":"53","author":"Eckhard","year":"2007","journal-title":"Electrochim. Acta"}],"container-title":["Biosensors"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-6374\/14\/11\/562\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:36:01Z","timestamp":1760114161000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-6374\/14\/11\/562"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,20]]},"references-count":98,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2024,11]]}},"alternative-id":["bios14110562"],"URL":"https:\/\/doi.org\/10.3390\/bios14110562","relation":{},"ISSN":["2079-6374"],"issn-type":[{"value":"2079-6374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,11,20]]}}}