Bioelectrocatalytic performance of d-fructose dehydrogenase

Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

“…It has been reported that some FDH variants show better DET-type bioelectrocatalytic performance than the wild-type (or recombinant native) FDH [28]. Considering the comparison of the formal potentials of hemes c and the onset potential of the steady-state catalytic wave of the DET-type bioelectrocatalysis, it was suggested that electrons were transferred from d-fructose to an electrode via FAD, heme 3c, and 2c in this order, and heme 1c seemed to be uninvolved in the intramolecular electron transfer in the DET-type reaction, as shown in Figure 9 [32].…”

“…Membrane-bound d-fructose dehydrogenase (FDH) is one DET-type redox enzyme [28]. FDH is a heterotrimer with a molecular mass of 138 kDa that is composed of three subunits; subunit I (67 kDa) contains a covalently bound flavin adenine dinucleotide (FAD) and oxidizes d-fructose to 5-keto-d-fructose, subunit II (51 kDa) includes three hemes c (heme 1c, 2c, and 3c from the N-terminus), and subunit III (20 kDa) exhibits a chaperonic function [29].…”

“…The electrons are transferred from substratereduced FAD to heme 3c, heme 2c, and an electrode without going to heme 1c. Reprinted from[28], Copyright (2019), with permission from Elsevier.…”

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

“…Bioelectrocatalysis has also found application in fuel cells. Reviews concerning the bioelectrocatalysis of specific classes of proteins have recently appeared, [16,[25][26][27] yet only a few focus on hemeproteins and on the multiple roles that these species can play in chemical and technological fields, from sensors to fuel cell development. [19][20][21][22][23][24] Heme proteins, a large protein family including redox enzymes, ET proteins and O 2 transport and storage species, possess a large functional versatility and can easily be engineered.…”

“…For these reasons, they have largely been employed in bio(in)organic interfaces for sensing and catalysis either in their native or mutated form. Reviews concerning the bioelectrocatalysis of specific classes of proteins have recently appeared, [16,[25][26][27] yet only a few focus on hemeproteins and on the multiple roles that these species can play in chemical and technological fields, from sensors to fuel cell development. The goal of this minireview is to provide an overview on the latest achievements in the field of heme protein-based bioelectrocatalysis, to help the reader perceive the opportunities offered by these systems and figure out how to exploit their applicative potential.…”