{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T22:28:14Z","timestamp":1778106494507,"version":"3.51.4"},"reference-count":170,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2018,4,24]],"date-time":"2018-04-24T00:00:00Z","timestamp":1524528000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sensors"],"abstract":"<jats:p>Dehydrogenase based bioelectrocatalysis has been increasingly exploited in recent years in order to develop new bioelectrochemical devices, such as biosensors and biofuel cells, with improved performances. In some cases, dehydrogeases are able to directly exchange electrons with an appropriately designed electrode surface, without the need for an added redox mediator, allowing bioelectrocatalysis based on a direct electron transfer process. In this review we briefly describe the electron transfer mechanism of dehydrogenase enzymes and some of the characteristics required for bioelectrocatalysis reactions via a direct electron transfer mechanism. Special attention is given to cellobiose dehydrogenase and fructose dehydrogenase, which showed efficient direct electron transfer reactions. An overview of the most recent biosensors and biofuel cells based on the two dehydrogenases will be presented. The various strategies to prepare modified electrodes in order to improve the electron transfer properties of the device will be carefully investigated and all analytical parameters will be presented, discussed and compared.<\/jats:p>","DOI":"10.3390\/s18051319","type":"journal-article","created":{"date-parts":[[2018,4,25]],"date-time":"2018-04-25T03:22:45Z","timestamp":1524626565000},"page":"1319","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":100,"title":["Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells"],"prefix":"10.3390","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9049-6406","authenticated-orcid":false,"given":"Paolo","family":"Bollella","sequence":"first","affiliation":[{"name":"Department of Chemistry and Drug Technologies, Sapienza University of Rome P.le Aldo Moro 5, 00185 Rome, Italy"}]},{"given":"Lo","family":"Gorton","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Structural Biology, Lund University, P.O. Box 124, 221 00 Lund, Sweden"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8990-8506","authenticated-orcid":false,"given":"Riccarda","family":"Antiochia","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Drug Technologies, Sapienza University of Rome P.le Aldo Moro 5, 00185 Rome, Italy"}]}],"member":"1968","published-online":{"date-parts":[[2018,4,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Canuto, R.A. (2012). Amperometric glucose sensors for whole blood measurement based on dehydrogenase enzymes. Dehydrogenases, InTechOpen.","DOI":"10.5772\/2903"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0079-6107(97)00020-5","article-title":"The structure and function of the PQQ-containing quinoprotein dehydrogenases","volume":"69","author":"Anthony","year":"1998","journal-title":"Prog. Biophys. Mol. 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