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

被引：40

作者：

Adachi, Taiki ^{[1
]}

Kitazumi, Yuki ^{[1
]}

Shirai, Osamu ^{[1
]}

Kano, Kenji ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Sakyo Ku, Kyoto 6068502, Japan

来源：

CATALYSTS | 2020年 / 10卷 / 02期

关键词：

direct electron transfer-type bioelectrocatalysis; nanostructures; mesoporous electrodes; curvature effect; protein engineering; bidirectional bioelectrocatalysis; D-FRUCTOSE DEHYDROGENASE; THERMOSTABLE GLUCOSE-DEHYDROGENASE; NANOPOROUS GOLD ELECTRODES; MGO-TEMPLATED CARBON; BILIRUBIN OXIDASE; HISTAMINE DEHYDROGENASE; DIRECT ELECTROCHEMISTRY; CATALYTIC SUBUNIT; BIOFUEL CELLS; FUEL-CELL;

D O I：

10.3390/catal10020236

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Direct electron transfer (DET)-type bioelectrocatalysis, which couples the electrode reactions and catalytic functions of redox enzymes without any redox mediator, is one of the most intriguing subjects that has been studied over the past few decades in the field of bioelectrochemistry. In order to realize the DET-type bioelectrocatalysis and improve the performance, nanostructures of the electrode surface have to be carefully tuned for each enzyme. In addition, enzymes can also be tuned by the protein engineering approach for the DET-type reaction. This review summarizes the recent progresses in this field of the research while considering the importance of nanostructure of electrodes as well as redox enzymes. This review also describes the basic concepts and theoretical aspects of DET-type bioelectrocatalysis, the significance of nanostructures as scaffolds for DET-type reactions, protein engineering approaches for DET-type reactions, and concepts and facts of bidirectional DET-type reactions from a cross-disciplinary viewpoint.

引用

页数：20

共 95 条

[1] Bioelectrocatalytic performance of D-fructose dehydrogenase [J].

Adachi, Taiki ;

Kaida, Yuya ;

Kitazumi, Yuki ;

Shirai, Osamu ;

Kano, Kenji .

BIOELECTROCHEMISTRY, 2019, 129 :1-9

[2] Construction of a bioelectrochemical formate generating system from carbon dioxide and dihydrogen [J].

Adachi, Taiki ;

Kitazumi, Yuki ;

Shirai, Osamu ;

Kano, Kenji .

ELECTROCHEMISTRY COMMUNICATIONS, 2018, 97 :73-76

[3] Highly Efficient Flavin-Adenine Dinucleotide Glucose Dehydrogenase Fused to a Minimal Cytochrome C Domain [J].

Algov, Itay ;

Grushka, Jennifer ;

Zarivach, Raz ;

Alfonta, Lital .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2017, 139 (48) :17217-17220

[4] Hydrogenase-coated carbon nanotubes for efficient H2 oxidation [J].

Alonso-Lomillo, M. Asuncion ;

Rudiger, Olaf ;

Maroto-Valiente, Angel ;

Velez, Marisela ;

Rodriguez-Ramos, Inmaculada ;

Munoz, F. Javier ;

Fernandez, Victor M. ;

De Lacey, Antonio L. .

NANO LETTERS, 2007, 7 (06) :1603-1608

[5]

[Anonymous], 2001, ELECTROCHEMICAL METH

[6] Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes [J].

Armstrong, Fraser A. ;

Hirst, Judy .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (34) :14049-14054

[7]

Bartlett P.N., 2008, BIOELECTROCHEMISTRY

[8] Enzymatic biofuel cells for Implantable and microscale devices [J].

Barton, SC ;

Gallaway, J ;

Atanassov, P .

CHEMICAL REVIEWS, 2004, 104 (10) :4867-4886

[9] Reversible lnterconversion of CO2 and Formate by a Molybdenum-Containing Formate Dehydrogenase [J].

Bassegoda, Arnau ;

Madden, Christopher ;

Wakerley, David W. ;

Reisner, Erwin ;

Hirst, Judy .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2014, 136 (44) :15473-15476

[10] Enzyme based amperometric biosensors [J].

Bollella, Paolo ;

Gorton, Lo .

CURRENT OPINION IN ELECTROCHEMISTRY, 2018, 10 :157-173

← 1 2 3 4 5 6 7 8 9 10 →