Cytochrome B562: Electroactive Protein for Bioelectronics

Hiroyuki Sasabe; Taiji Furuno; Kazutoshi Kobayashi; Yukio Kobayashi; Teruyuki Nagamune

doi:10.1080/10587259408029798

Cytochrome B562: Electroactive Protein for Bioelectronics

Hiroyuki Sasabe, Taiji Furuno, Kazutoshi Kobayashi, Yukio Kobayashi, Teruyuki Nagamune

Research output: Contribution to journal › Article › peer-review

Abstract

To develop bioelectronic devices and/or the structural analyses of proteins, two-dimensional crystallization of proteins is required. Heme proteins are particularly interesting due to electron transfer characteristics associated with the porphyrin-based prosthetic group. Cytochrome b562 has been chosen as a model protein for the fabrication of two-dimensional crystals. Three approaches in making two-dimensional crystals of cytochrome b562 are presented here: (1) the formation of monomolecular layer of cytochrome b562 reconstituted with alkylated heme, (2) the control of surface charge density of cytochrome b562 and (3) the enhancement of thermal stability both by means of protein engineering.

Original language	English
Pages (from-to)	271-278
Number of pages	8
Journal	Molecular Crystals and Liquid Crystals Science and Technology. Section A. Molecular Crystals and Liquid Crystals
Volume	255
Issue number	1
DOIs	https://doi.org/10.1080/10587259408029798
Publication status	Published - 1994 Oct
Externally published	Yes

ASJC Scopus subject areas

Condensed Matter Physics

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10.1080/10587259408029798

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abstract = "To develop bioelectronic devices and/or the structural analyses of proteins, two-dimensional crystallization of proteins is required. Heme proteins are particularly interesting due to electron transfer characteristics associated with the porphyrin-based prosthetic group. Cytochrome b562 has been chosen as a model protein for the fabrication of two-dimensional crystals. Three approaches in making two-dimensional crystals of cytochrome b562 are presented here: (1) the formation of monomolecular layer of cytochrome b562 reconstituted with alkylated heme, (2) the control of surface charge density of cytochrome b562 and (3) the enhancement of thermal stability both by means of protein engineering.",

author = "Hiroyuki Sasabe and Taiji Furuno and Kazutoshi Kobayashi and Yukio Kobayashi and Teruyuki Nagamune",

year = "1994",

month = oct,

doi = "10.1080/10587259408029798",

language = "English",

volume = "255",

pages = "271--278",

journal = "Molecular Crystals and Liquid Crystals",

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TY - JOUR

T1 - Cytochrome B562

T2 - Electroactive Protein for Bioelectronics

AU - Sasabe, Hiroyuki

AU - Furuno, Taiji

AU - Kobayashi, Kazutoshi

AU - Kobayashi, Yukio

AU - Nagamune, Teruyuki

PY - 1994/10

Y1 - 1994/10

N2 - To develop bioelectronic devices and/or the structural analyses of proteins, two-dimensional crystallization of proteins is required. Heme proteins are particularly interesting due to electron transfer characteristics associated with the porphyrin-based prosthetic group. Cytochrome b562 has been chosen as a model protein for the fabrication of two-dimensional crystals. Three approaches in making two-dimensional crystals of cytochrome b562 are presented here: (1) the formation of monomolecular layer of cytochrome b562 reconstituted with alkylated heme, (2) the control of surface charge density of cytochrome b562 and (3) the enhancement of thermal stability both by means of protein engineering.

AB - To develop bioelectronic devices and/or the structural analyses of proteins, two-dimensional crystallization of proteins is required. Heme proteins are particularly interesting due to electron transfer characteristics associated with the porphyrin-based prosthetic group. Cytochrome b562 has been chosen as a model protein for the fabrication of two-dimensional crystals. Three approaches in making two-dimensional crystals of cytochrome b562 are presented here: (1) the formation of monomolecular layer of cytochrome b562 reconstituted with alkylated heme, (2) the control of surface charge density of cytochrome b562 and (3) the enhancement of thermal stability both by means of protein engineering.

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ER -

Cytochrome B562: Electroactive Protein for Bioelectronics

Abstract

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