d-Fructose dehydrogenase (FDH), a membrane-bound heterotrimeric enzyme, shows strong activity in direct electron transfer (DET)-type bioelectrocatalysis. An FDH variant (Δ1c2cFDH) which lacks 199 amino acid residues including two heme c moieties from N-terminus was constructed, and its DET-type bioelectrocatalytic performance was evaluated with cyclic voltammetry at Au planar electrodes. A DET-type catalytic current of d-fructose oxidation was clearly observed on Δ1c2cFDH-adsorbed Au electrodes. Detailed analysis of the steady-state catalytic current indicated that Δ1c2cFDH transports the electrons to the electrode via heme 3c at a more negative potential and at more improved kinetics than the recombinant (native) FDH.

d-果糖脱氢酶（FDH）是一种膜结合的异三聚酶，在直接电子转移（DET）型生物电催化中显示出强大的活性。一个FDH变体（Δ1 c ^ 2 Ç FDH）其缺乏199个氨基酸残基包括二血红素Ç从N-末端部分，构建，并与在凹平面电极循环伏安其DET型生物电催化性能进行评价。的DET型催化电流d -fructose氧化清楚地观察到在Δ1 ç 2 ç FDH吸附的Au电极。稳态催化电流的详细分析表明，Δ1 Ç 2 ÇFDH通过血红素3c将电子以比重组（天然）FDH更高的负电势和更好的动力学传输到电极。