Literature DB >> 7576441

The design of enzyme sensors based on the enzyme structure.

M Alvarez-Icaza1, H M Kalisz, H J Hecht, K D Aumann, D Schomburg, R D Schmid.   

Abstract

The size of some of the reported electron mediators for glucose oxidase compared with the available space to penetrate the active site, implies that electrons have to move along the protein structure. Theoretical and experimental evidence predicts that it is possible to have electron transfer at the required rate used in biosensors (200 to 1840 electrons s-1) for the distances in glucose oxidase (20 to 25 A). Use of the program "Pathways" (together with the knowledge of the enzyme structure) allowed us to find an electron pathway within the enzyme. This pathway has a maximum electron coupling between the active site and the surface of the enzyme. The pathway reaches the surface near functional groups that can be used for oriented immobilization of the enzyme. Experimental confirmation of this particular pathway has been attempted but it is still elusive.

Mesh:

Substances:

Year:  1995        PMID: 7576441     DOI: 10.1016/0956-5663(95)96964-z

Source DB:  PubMed          Journal:  Biosens Bioelectron        ISSN: 0956-5663            Impact factor:   10.618


  3 in total

1.  Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli.

Authors:  S Witt; M Singh; H M Kalisz
Journal:  Appl Environ Microbiol       Date:  1998-04       Impact factor: 4.792

Review 2.  Electrochemical glucose sensors--developments using electrostatic assembly and carbon nanotubes for biosensor construction.

Authors:  Alice Harper; Mark R Anderson
Journal:  Sensors (Basel)       Date:  2010-09-02       Impact factor: 3.576

Review 3.  Enzyme-Based Biosensors: Tackling Electron Transfer Issues.

Authors:  Paolo Bollella; Evgeny Katz
Journal:  Sensors (Basel)       Date:  2020-06-21       Impact factor: 3.576

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.