Manipulating redox systems: application to nanotechnology

被引:98
作者
Gilardi, G [1 ]
Fantuzzi, A [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AY, England
基金
英国生物技术与生命科学研究理事会;
关键词
D O I
10.1016/S0167-7799(01)01769-3
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Redox proteins and enzymes are attractive targets for nanobiotechnology. The theoretical framework of biological electron transfer is increasingly well-understood, and several properties make redox centres good systems for exploitation: many can be detected both electrochemically and optically; they can perform specific reactions; they are capable of self-assembly; and their dimensions are in the nanoscale. Great progress has been made with the,two main approaches of protein engineering: rational design and combinatorial synthesis. Rational design has put our understanding of the structure-function relationship to the test, whereas combinatorial synthesis has generated new molecules of interest. This article provides selected examples of novel approaches where redox proteins are 'wired up' in efficient electron-transfer chains, are 'assembled' in artificial multidomain structures (molecular Lego), are 'linked' to surfaces in nanodevices for biosensing and nanobiotechnological applications.
引用
收藏
页码:468 / 476
页数:9
相关论文
共 53 条
[21]  
GILARDI G, IN PRESS BIOSENS BIO
[22]   Efficient mediatorless superoxide sensors using cytochrome c-modified electrodes:: surface nano-organization for selectivity and controlled peroxidase activity [J].
Gobi, KV ;
Mizutani, F .
JOURNAL OF ELECTROANALYTICAL CHEMISTRY, 2000, 484 (02) :172-181
[23]   Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors [J].
Gorton, L ;
Lindgren, A ;
Larsson, T ;
Munteanu, FD ;
Ruzgas, T ;
Gazaryan, I .
ANALYTICA CHIMICA ACTA, 1999, 400 :91-108
[24]   Electron transfer in proteins [J].
Gray, HB ;
Winkler, JR .
ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :537-561
[25]   Electrooxidation of phenol by catalase immobilized on graphite electrodes [J].
Horozova, E ;
Dimcheva, N ;
Jordanova, Z .
BIOELECTROCHEMISTRY, 2001, 53 (01) :11-16
[26]   Redox-active lipid-incorporating proteins as a novel immobilisation technique [J].
Jacob, C ;
Safronov, AY ;
Wilson, S ;
Hill, HAO ;
Booth, TF ;
Chapman, SK .
JOURNAL OF ELECTROANALYTICAL CHEMISTRY, 1997, 430 (1-2) :119-125
[27]   Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: The electron-transfer and redox-coupled ligand binding properties of His117Gly azurin [J].
Jeuken, LJC ;
van Vliet, P ;
Verbeet, MP ;
Camba, R ;
McEvoy, JP ;
Armstrong, FA ;
Canters, GW .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (49) :12186-12194
[28]   PROTEIN DESIGN BY BINARY PATTERNING OF POLAR AND NONPOLAR AMINO-ACIDS [J].
KAMTEKAR, S ;
SCHIFFER, JM ;
XIONG, HY ;
BABIK, JM ;
HECHT, MH .
SCIENCE, 1993, 262 (5140) :1680-1685
[29]   Effect of the microenvironment on the recognition of immobilized cytochromes by soluble redox proteins [J].
Kloss, AA ;
Lavrik, N ;
Yeung, C ;
Leckband, D .
LANGMUIR, 2000, 16 (07) :3414-3421
[30]   A fullerene-modified protein [J].
Kurz, A ;
Halliwell, CM ;
Davis, JJ ;
Hill, HAO ;
Canters, GW .
CHEMICAL COMMUNICATIONS, 1998, (03) :433-434