JPH0770764B2 - Switch element - Google Patents
Switch elementInfo
- Publication number
- JPH0770764B2 JPH0770764B2 JP61155450A JP15545086A JPH0770764B2 JP H0770764 B2 JPH0770764 B2 JP H0770764B2 JP 61155450 A JP61155450 A JP 61155450A JP 15545086 A JP15545086 A JP 15545086A JP H0770764 B2 JPH0770764 B2 JP H0770764B2
- Authority
- JP
- Japan
- Prior art keywords
- electron transfer
- switch element
- electron
- film
- transfer material
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 230000027756 respiratory electron transport chain Effects 0.000 claims description 134
- 102000004169 proteins and genes Human genes 0.000 claims description 100
- 108090000623 proteins and genes Proteins 0.000 claims description 100
- 239000000463 material Substances 0.000 claims description 31
- 239000000126 substance Substances 0.000 claims description 28
- 239000002184 metal Substances 0.000 claims description 8
- 229910052751 metal Inorganic materials 0.000 claims description 8
- 239000012620 biological material Substances 0.000 claims description 6
- 102100030497 Cytochrome c Human genes 0.000 claims description 5
- 108010075031 Cytochromes c Proteins 0.000 claims description 5
- 125000002524 organometallic group Chemical group 0.000 claims description 5
- 108010075027 Cytochromes a Proteins 0.000 claims description 4
- 150000001413 amino acids Chemical class 0.000 claims description 4
- 235000014113 dietary fatty acids Nutrition 0.000 claims description 4
- 229930195729 fatty acid Natural products 0.000 claims description 4
- 239000000194 fatty acid Substances 0.000 claims description 4
- 150000004665 fatty acids Chemical class 0.000 claims description 4
- 229920000642 polymer Polymers 0.000 claims description 4
- 102100025287 Cytochrome b Human genes 0.000 claims description 3
- 108010075028 Cytochromes b Proteins 0.000 claims description 3
- 102000004190 Enzymes Human genes 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 3
- 108010057366 Flavodoxin Proteins 0.000 claims description 3
- 150000003862 amino acid derivatives Chemical class 0.000 claims description 3
- 230000001747 exhibiting effect Effects 0.000 claims description 3
- XEEYBQQBJWHFJM-UHFFFAOYSA-N iron Substances [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims description 3
- 150000002632 lipids Chemical class 0.000 claims description 3
- 238000006479 redox reaction Methods 0.000 claims description 3
- 108090000051 Plastocyanin Proteins 0.000 claims description 2
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 claims description 2
- 102000002933 Thioredoxin Human genes 0.000 claims description 2
- 229910052742 iron Inorganic materials 0.000 claims description 2
- 229910052717 sulfur Inorganic materials 0.000 claims description 2
- 239000011593 sulfur Substances 0.000 claims description 2
- 238000010189 synthetic method Methods 0.000 claims description 2
- 108060008226 thioredoxin Proteins 0.000 claims description 2
- 229940094937 thioredoxin Drugs 0.000 claims description 2
- 239000010408 film Substances 0.000 description 36
- 239000012528 membrane Substances 0.000 description 26
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 14
- 238000010586 diagram Methods 0.000 description 11
- 239000000758 substrate Substances 0.000 description 11
- 238000000034 method Methods 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 239000010409 thin film Substances 0.000 description 6
- 210000003470 mitochondria Anatomy 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- UHOVQNZJYSORNB-UHFFFAOYSA-N Benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 3
- 230000001186 cumulative effect Effects 0.000 description 3
- 239000010410 layer Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 102000035118 modified proteins Human genes 0.000 description 3
- 108091005573 modified proteins Proteins 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 239000004065 semiconductor Substances 0.000 description 3
- 229910052710 silicon Inorganic materials 0.000 description 3
- -1 2,2'-bipyridylyl Chemical group 0.000 description 2
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 239000000084 colloidal system Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 230000005669 field effect Effects 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 239000010703 silicon Substances 0.000 description 2
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 2
- KDYFGRWQOYBRFD-UHFFFAOYSA-N succinic acid Chemical compound OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 2
- MWVTWFVJZLCBMC-UHFFFAOYSA-N 4,4'-bipyridine Chemical group C1=NC=CC(C=2C=CN=CC=2)=C1 MWVTWFVJZLCBMC-UHFFFAOYSA-N 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 108091006149 Electron carriers Proteins 0.000 description 1
- 102000000490 Mediator Complex Human genes 0.000 description 1
- 108010080991 Mediator Complex Proteins 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- DFPAKSUCGFBDDF-UHFFFAOYSA-N Nicotinamide Chemical compound NC(=O)C1=CC=CN=C1 DFPAKSUCGFBDDF-UHFFFAOYSA-N 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 1
- 229910004298 SiO 2 Inorganic materials 0.000 description 1
- 108050006628 Viral movement proteins Proteins 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000006356 dehydrogenation reaction Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 238000009413 insulation Methods 0.000 description 1
- 238000010884 ion-beam technique Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000001384 succinic acid Substances 0.000 description 1
- 239000002344 surface layer Substances 0.000 description 1
- 239000011882 ultra-fine particle Substances 0.000 description 1
- 238000007740 vapor deposition Methods 0.000 description 1
Landscapes
- Bipolar Transistors (AREA)
Description
【発明の詳細な説明】 〔産業上の利用分野〕 この発明は、集積回路分野におけるスイッチ素子に関す
るもので、生体材料を該素子の構成材料として用いるこ
とにより、そのサイズを生体分子レベルの超微細な大き
さ（数十〜数百Å）に近づけることができ、高密度化，
高速化を図ることができるようにしたものである。Description: TECHNICAL FIELD The present invention relates to a switch element in the field of integrated circuits. By using a biomaterial as a constituent material of the element, its size can be reduced to ultrafine particles at a biomolecule level. Size (several tens to hundreds of Å) can be approached, and high density,
This is to enable speeding up.
従来、集積回路に用いられているスイッチ素子として
は、第７図に示す電界効果型トランジスタ（FET）があ
った。図において、１はｎ形シリコン基板、２はチャン
ネル領域、３はP+層、４はSiO2膜、５はソース電極、６
はゲート電極、７はドレイン電極であり、この従来のFE
Tをトランジスタ動作又はスイッチング動作させるに
は、ゲート電極に印加するゲート電圧の制御により行
う。即ち、ゲート電圧によってソース電極５とドレイン
電極７間の表面層における電流キャリア数を変化させれ
ば、これにより電流が制御される。Conventionally, a field effect transistor (FET) shown in FIG. 7 has been used as a switching element used in an integrated circuit. In the figure, 1 is an n-type silicon substrate, 2 is a channel region, 3 is a P + layer, 4 is a SiO 2 film, 5 is a source electrode, and 6
Is a gate electrode, and 7 is a drain electrode.
The transistor operation or the switching operation of T is performed by controlling the gate voltage applied to the gate electrode. That is, if the number of current carriers in the surface layer between the source electrode 5 and the drain electrode 7 is changed by the gate voltage, the current is controlled by this.
従来のスイッチ素子は以上のように構成されているた
め、微細加工が可能であり、現在では上記構造のスイッ
チ素子あるいはこれと類似の構造の整流素子を用いたLS
Iとして256KビットLSIが実用化されている。Since the conventional switch element is configured as described above, it can be microfabricated, and at present, the LS using the switch element having the above structure or a rectifying element having a similar structure to this is used.
A 256K-bit LSI has been put to practical use as I.
ところで、集積回路のメモリ容量と演算速度を上昇させ
るには、素子そのものの微細化が不可欠であるが、Siを
用いる素子では0.2μｍ程度の超微細パターンで電子の
平均自由行程と素子サイズとがほぼ等しくなり、素子の
独立性が保たれなくなるという限界を抱えている。この
ように、日々発展を続けているシリコンテクノロジー
も、微細化の点ではいずれは壁にある突きあたることが
予想され、新しい原理に基づく電気回路素子であって上
記0.2μｍの壁を越える新しい原理に基づくVLSIが求め
られている。By the way, in order to increase the memory capacity and operation speed of an integrated circuit, it is indispensable to miniaturize the element itself. However, in the element using Si, the average free path and the element size of the electron are reduced by an ultrafine pattern of about 0.2 μm. There is a limit that they become almost equal and the independence of elements cannot be maintained. In this way, silicon technology, which continues to develop day by day, is expected to eventually hit the wall in terms of miniaturization, and it is an electric circuit element based on a new principle, which is a new principle that exceeds the 0.2 μm wall. VLSI based on is required.
この発明は、かかる状況に鑑みてなされたもので、生体
材料を電気回路素子の構成材料として用いることによ
り、そのサイズを生体分子レベルの超微細な大きさにま
で近づけることのできる電気回路素子を、特にそのうち
のスイッチ素子を提供することを目的とする。The present invention has been made in view of the above circumstances, and by using a biomaterial as a constituent material of an electric circuit element, an electric circuit element capable of approaching its size to an ultrafine size at a biomolecule level is provided. In particular, it is intended to provide a switching element of them.
ところで、微生物の生体膜及び高等生物のミトコンドリ
アの内膜中には、それぞれ機能は異なるが、H2,有機酸,
NAD（Ｐ）Ｈ（Nicotineamide Adenine Dinucleotide（P
hosphate））などの還元性の化学物質から電子を引き抜
く酵素蛋白質とともに、その引き抜かれた電子を生体膜
の定められた方向に運ぶ電子伝達能を有する蛋白質（以
下電子蛋白質と記す）が複数種類存在している。そして
これらの電子伝達蛋白質は生体膜中に一定の配向性をも
って埋め込まれ、分子間で電子伝達が起こるように特異
的な分子間配置をとっている。By the way, in the biological membranes of microorganisms and the inner membranes of mitochondria of higher organisms, H 2
NAD (P) H (Nicotineamide Adenine Dinucleotide (P
hosphate)) and other enzyme proteins that withdraw electrons from reductive chemicals, as well as multiple types of proteins (hereinafter referred to as electronic proteins) that have the ability to transfer electrons that have been withdrawn to defined directions in biological membranes. is doing. These electron transfer proteins are embedded in the biological membrane with a certain orientation, and have a specific intermolecular arrangement so that electron transfer occurs between the molecules.
このように、電子伝達蛋白質は生体膜中で精巧な配置を
もって連鎖状に並んでいるため、これを利用すれば電子
の動き分子レベルで制御することができると考えられ
る。As described above, since electron transfer proteins are arranged in a chain in a biological membrane with delicate arrangement, it is considered that electron movement proteins can be controlled at the molecular level of electrons.
第６図に電子伝達蛋白質の連鎖（電子伝達系）の一例と
して、ミトコンドリアの内膜の電子伝達系を模式的に示
す。図において、８はミトコンドリアの内膜、９〜15は
電子伝達蛋白質であり、還元性有機物であるNADH（図中
Ｌ），コハク酸（図中Ｍ）からそれぞれNADH−Ｑ還元酵
素9,コハク酸脱水素酵素10により引き抜かれた電子は、
NADH−Ｑ還元酵素9,コハク酸脱水素酸素10→チトクロー
ムｂ（11）→チトクロームc1（12）→チトクロームｃ
（13）→チトクロームａ（14）→チトクロームa3（15）
の経路で伝達し、出口側Ｎで最終的に酸素を渡され、水
を生ずる。FIG. 6 schematically shows an electron transfer system of the inner membrane of mitochondria as an example of a chain of electron transfer proteins (electron transfer system). In the figure, 8 is an inner membrane of mitochondria, 9 to 15 are electron transfer proteins, and NADH-Q reductase 9 and succinate are converted from reducing organic substances such as NADH (L in the figure) and succinic acid (M in the figure), respectively. The electrons extracted by the dehydrogenase 10 are
NADH-Q reductase 9, succinate dehydrogenation oxygen 10 → cytochrome b (11) → cytochrome c 1 (12) → cytochrome c
(13) → Cytochrome a (14) → Cytochrome a 3 (15)
And is finally passed oxygen at the outlet side N to produce water.
第６図に示した電子伝達蛋白質は電子伝達時に酸化還元
（レドックス）反応を伴い、各電子伝達蛋白質のレドッ
クス電位の負の準位から正の準位へと電子を流すことが
できる。The electron transfer protein shown in FIG. 6 is accompanied by a redox reaction at the time of electron transfer, and electrons can flow from the negative level of the redox potential of each electron transfer protein to the positive level.
また、最近の知見によれば、同一生体内に存在している
電子伝達蛋白質ばかりでなく、異種の生体内に存在する
電子伝達蛋白質を組み合わせても電子伝達が可能な電子
伝達蛋白質複合体を形成することが可能であることが示
されている。According to recent findings, not only electron transfer proteins existing in the same living body but also electron transfer proteins existing in different living bodies are combined to form electron transfer protein complexes capable of electron transfer. Has been shown to be possible.
従って、適当なレドックス電位を持つ電子伝達蛋白質を
２種類（Ａ及びＢ）用い、Ａ−Ｂ−Ａと３層累積させれ
ば、それらのレドックス電位の違いを利用してトランジ
スタ特性又はスイッチング特性を生ずる接合を形成でき
ると考えられる。本発明者はこのことに着目してこの発
明を創作したものである。Therefore, if two types of electron transfer proteins (A and B) having an appropriate redox potential are used and three layers are accumulated with A-B-A, the transistor characteristics or switching characteristics can be improved by utilizing the difference in redox potential. It is believed that the resulting bond can be formed. The present inventor has created this invention with this in mind.
即ち、本発明に係るスイッチ素子は、天然に存在する電
子伝達蛋白質を化学的に改変したり、またそれを模倣し
てなる第１電子伝達物質で作成された第１電子伝達物質
膜と、上記第１電子伝達物質のレドックス（酸化還元）
電位と異なるレドックス電位を有する第２電子伝達物質
で作成され、上記第１電子伝達物質膜に累積して接着接
合された第２電子伝達物質膜と、上記第２電子伝達物質
膜のレドックス電位と異なるレドックス電位を有する第
３電子伝達物質で作成され、上記第２電子伝達物質膜に
累積して接着接合された第３電子伝達物質膜と、それぞ
れ上記第1,第2,第３電子伝達物質に接続される第1,第2,
第３の電極とを設けたものである。That is, the switch element according to the present invention comprises a first electron mediator film made of a first electron mediator that chemically modifies or naturally mimics a naturally occurring electron carrier protein; Redox (redox) of the first electron transfer substance
A second electron messenger film made of a second electron messenger material having a redox potential different from the potential and accumulated and bonded to the first electron messenger film; and a redox potential of the second electron messenger film. A third electron transfer material film made of third electron transfer materials having different redox potentials and accumulated and bonded to the second electron transfer material film, and the first, second and third electron transfer materials respectively. Connected to the first, second,
And a third electrode.
この発明においては、レドックス電位の異なる少なくと
も２種類の電子伝達物質はトランジスタ特性又はスイッ
チング特性を呈する。即ち、第５図（ａ），（ｂ）に示
すＡ−Ｂ−Ａ型電子伝達物質複合体の模式図とそのレド
ックス電位の関係を用いて説明すると、この電子伝達物
質A,B,Aを接合してなる複合体では、A,B,A蛋白質のレド
ックス電位の分布をＢ蛋白質への印加電圧を制御して変
化させることができ、これによりｎ型半導体とｐ型半導
体とを接合してなるｐ−ｎ−ｐ接合と類似のトランジス
タ特性又はスイッチング特性を呈する素子を得ることが
できる。In the present invention, at least two kinds of electron transfer substances having different redox potentials exhibit transistor characteristics or switching characteristics. That is, using the schematic diagram of the ABA type electron mediator complex shown in FIGS. 5 (a) and 5 (b) and the relationship between the redox potentials thereof, the electron mediators A, B, and A will be described. In the complex formed by conjugation, the distribution of the redox potential of A, B, and A protein can be changed by controlling the applied voltage to B protein, and thereby the n-type semiconductor and the p-type semiconductor are joined. An element exhibiting transistor characteristics or switching characteristics similar to the p-n-p junction can be obtained.
以下、本願の第１の発明の実施例を図について説明す
る。第１図はこの発明の一実施例によるスイッチ素子が
組み込まれた装置の模式的断面構成図であり、図におい
て、16は絶縁特性を持つ基板、17はAg,Au,Alなどの金属
製電極で、基板16上に複数条が平行に形成されている。
18は第１の改変電子伝達蛋白質で作成された第１電子伝
達蛋白質膜で、この第１の改変電子伝達蛋白質は、フラ
ボドキシン等の天然電子伝達蛋白質にアミノ酸を結合し
たり、また−ＨをＦやCH3に，あるいはＣをSi等に置換
したアミノ酸誘導体を結合してなるものである。20は上
記複数条の平行電極17と直角方向に形成された複数条の
平行電極であり、上記第１電子伝達蛋白質膜18上に形成
されている。19は上記第１の改変電子伝達蛋白質のレド
ックス電位と異なるレドックス電位を有する第２の改変
電子伝達蛋白質で作成された第２電子伝達蛋白質膜で、
上記第１電子伝達蛋白質18に累積して接着接合され、電
極20に接合されている。この第２の改変電子伝達蛋白質
も上記と同様に天然電子伝達蛋白質を改変してなるもの
である。21は上記第１の改変電子伝達蛋白質で作成され
た第３電子伝達蛋白質膜で、上記第２電子伝達蛋白質膜
19上に累積して接着接合されている。22は複数条の平行
電極20と直角方向に形成された複数条の平行電極で、第
３電子伝達蛋白質膜21上に形成されている。第２図は形
成したスイッチ素子を組み込んだ装置を分解して示す分
解斜視図である。Embodiments of the first invention of the present application will be described below with reference to the drawings. FIG. 1 is a schematic cross-sectional configuration diagram of an apparatus incorporating a switch element according to an embodiment of the present invention. In the figure, 16 is a substrate having insulating properties, 17 is a metal electrode such as Ag, Au, Al. Thus, a plurality of lines are formed in parallel on the substrate 16.
18 is a first electron transfer protein membrane made of the first modified electron transfer protein. This first modified electron transfer protein binds an amino acid to a natural electron transfer protein such as flavodoxin or -H Or CH 3 or an amino acid derivative in which C is replaced by Si or the like is bound. Reference numeral 20 denotes a plurality of parallel electrodes formed in a direction perpendicular to the plurality of parallel electrodes 17 and is formed on the first electron transfer protein film 18. 19 is a second electron transfer protein membrane made of a second modified electron transfer protein having a redox potential different from the redox potential of the first modified electron transfer protein,
The first electron transfer protein 18 is accumulated and adhesively bonded to the electrode 20. This second modified electron transfer protein is also a modification of the natural electron transfer protein as described above. Reference numeral 21 is a third electron transfer protein membrane made of the first modified electron transfer protein, and the second electron transfer protein membrane
Cumulatively glued and bonded on top of 19. Reference numeral 22 is a plurality of parallel electrodes formed in a direction perpendicular to the plurality of parallel electrodes 20 and is formed on the third electron transfer protein film 21. FIG. 2 is an exploded perspective view showing the apparatus incorporating the formed switch element in an exploded manner.
このように構成された本実施例のスイッチ素子は、第１
図に示すような一定方向に電子伝達通路Ｅを有し、この
電子伝達通路Ｅと交わるように形成された電極17と22間
の電流の流れを、電極20に印加する電極によって制御す
るものである。The switch element of the present embodiment configured as described above has the first
An electron transfer passage E is provided in a fixed direction as shown in the figure, and a current flow between electrodes 17 and 22 formed so as to intersect with the electron transfer passage E is controlled by an electrode applied to the electrode 20. is there.
次に上記装置の製造方法について説明する。Next, a method of manufacturing the above device will be described.
まず、基板16上にイオンビーム法，分子線法，蒸着法等
を利用して金属薄膜を作成し、電極17を形成する。次に
上記改変電子伝達蛋白質（以下、単に電子伝達蛋白質と
記す）を用いて単分子膜及びそれらの累積膜を作成する
訳であるが、これらの膜を作成するには、LB（Langmuir
−Blodgett）法を用いればよい。このLB法の詳細につい
ては、電気学会雑誌，第55巻,204〜213頁，昭和10年
４月（Iwing Langmuir）、ジャーナル オブ アメリ
カン ケミカル ソサイティ（K.Blodgett:Journal of
American Chemical Society）57巻,P1007,1935年、杉
道夫ら，固体物理,Vol 17,P744〜752,1982年、ジャ
ーナル オブ コロイド アンド インターフェイス
サイエンスJournal of Colloid and Interface Scienc
e）Vol68,P471〜477,1979年、などに記載されている。
一例を説明すると、水槽の水面に第１の電子伝達蛋白質
の溶液を滴下し、水面に第１の電子伝達蛋白質の単分子
膜を形成する。この第１電子伝達蛋白質膜がが形成され
た水槽に電極17を形成した基板16を垂直に挿入し浸して
行くと、該電極17を有する基板16に第１電子伝達蛋白質
膜18が付着接合する。このとき、基板16を水槽に挿入し
浸していったが、逆に水面下から垂直に引き上げるよう
にして基板16上に第１電子伝達蛋白質膜18を形成するよ
うにしてもよい。First, a metal thin film is formed on the substrate 16 by using the ion beam method, the molecular beam method, the vapor deposition method or the like, and the electrode 17 is formed. Next, the above-mentioned modified electron transfer protein (hereinafter simply referred to as electron transfer protein) is used to prepare monomolecular films and their cumulative films. To prepare these films, LB (Langmuir
-Blodgett) method may be used. For details of this LB method, the Institute of Electrical Engineers of Japan, Vol. 55, p. 204-213, April 1952 (Iwing Langmuir), Journal of American Chemical Society (K.Blodgett: Journal of
American Chemical Society) 57, P1007, 1935, Michio Sugi et al., Solid State Physics, Vol 17, P744 ~ 752, 1982, Journal of Colloid and Interface.
Science Journal of Colloid and Interface Scienc
e) Vol68, P471-477, 1979, etc.
To explain one example, a solution of the first electron transfer protein is dropped on the water surface of the water tank to form a monomolecular film of the first electron transfer protein on the water surface. When the substrate 16 on which the electrode 17 is formed is vertically inserted and immersed in the water tank in which the first electron transfer protein film is formed, the first electron transfer protein film 18 is attached and bonded to the substrate 16 having the electrode 17. . At this time, the substrate 16 was inserted into the water tank and immersed, but the first electron transfer protein film 18 may be formed on the substrate 16 by pulling it up vertically from below the water surface.
次に上記と同様の方法で、上記第１電子伝達蛋白質膜18
上に上記電子伝達蛋白質が破壊されないほどの低温で電
極20を作成する。続いて、水槽の水面に第２の電子伝達
蛋白質の溶液を滴下し、水面に第２の電子伝達蛋白質の
単分子膜を形成する。そして上記第１電子伝達蛋白質膜
18及び電極20が作成された基板16を、第２電子伝達蛋白
質膜を有する水槽に垂直に挿入し浸して行くと、第１電
子伝達蛋白質膜18上に第２電子伝達蛋白質膜19が付着接
合し、電極20に接合した第２電子伝達蛋白質膜19が作成
される。同様にして基板16の第２電子伝達蛋白質膜19上
に第３電子伝達蛋白質膜21を作成し、さらにこの上に電
極22を作成する。Next, in the same manner as described above, the first electron transfer protein film 18
The electrode 20 is formed on the upper surface at a temperature low enough not to destroy the electron transfer protein. Then, the solution of the second electron transfer protein is dropped on the water surface of the water tank to form a monomolecular film of the second electron transfer protein on the water surface. And the first electron transfer protein membrane
When the substrate 16 on which the electrodes 18 and the electrodes 20 are formed is vertically inserted and immersed in a water tank having a second electron transfer protein film, the second electron transfer protein film 19 is attached and bonded onto the first electron transfer protein film 18. Then, the second electron transfer protein film 19 bonded to the electrode 20 is created. Similarly, the third electron transfer protein film 21 is formed on the second electron transfer protein film 19 of the substrate 16, and the electrode 22 is further formed thereon.
なお、上記電子伝達蛋白質膜は単分子膜であっても、ま
た別の改変電子伝達蛋白質の膜をこれに重ねたものであ
ってもよい。このとき、例えば第１電子伝達蛋白質膜を
２層累積して形成した場合は、これらの両電子伝達物質
間のレドックス電位差は、第1,第２電子伝達蛋白質膜間
のレドックス電位差より小さいものを選定する。The electron transfer protein film may be a monomolecular film, or may be a film of another modified electron transfer protein stacked thereon. At this time, for example, when two layers of the first electron transfer protein membrane are accumulated and formed, the redox potential difference between these two electron transfer substances should be smaller than the redox potential difference between the first and second electron transfer protein membranes. Select.
また、上記製法において水面に滴下する電子伝達蛋白質
溶液に脂質及び脂肪酸のいずれかを混合し、該混合溶液
を水面に滴下して水面に膜を形成し、これを基板に付着
接合させるようにしてもよく、これによれば上記脂質又
は脂肪酸が電子伝達蛋白質の分子の支持として作用し、
電子伝達蛋白質の配向が整えられる。Further, in the above production method, either the lipid or the fatty acid is mixed with the electron transfer protein solution to be dropped on the water surface, and the mixed solution is dropped on the water surface to form a film on the water surface, which is attached and bonded to the substrate. According to this, the above lipid or fatty acid acts as a support for the molecule of the electron transfer protein,
The orientation of the electron transfer protein is adjusted.
また、金属電極と電子伝達蛋白質膜間の電子の授受を良
好にするためには、金属電極を4,4′−ビピリジル（bip
yridgl）、2,2′−ビピリジリルなどで化学修飾してお
いてもよい。Further, in order to improve the transfer of electrons between the metal electrode and the electron transfer protein membrane, the metal electrode should be 4,4'-bipyridyl (bip
yridgl), 2,2'-bipyridylyl and the like may be chemically modified.
その他電子伝達蛋白質膜の作成法としては、金属電極あ
るいは有機分子で表面を修飾した金属電極を、改変した
電子伝達蛋白質等の溶液に浸漬して該改変蛋白質分子を
電極上に吸着させる方法も考えられる。この方法におい
ては、上記した電子伝達蛋白質を吸着させる電極以外に
１ないし２本の電極を溶液中に浸漬し、電子伝達蛋白質
を吸着させる電極と蛋白質溶液との間に正または負の電
位を印加して改変蛋白質分子の電極への吸着を制御する
ことも可能である。As another method for producing an electron transfer protein membrane, a method of immersing a metal electrode or a metal electrode whose surface is modified with an organic molecule in a solution of a modified electron transfer protein or the like to adsorb the modified protein molecule on the electrode is also considered. To be In this method, one or two electrodes other than the electrode for adsorbing the electron transfer protein are immersed in a solution, and a positive or negative potential is applied between the electrode for adsorbing the electron transfer protein and the protein solution. It is also possible to control the adsorption of the modified protein molecule on the electrode.
次に作用効果について説明する。Next, the function and effect will be described.
第１図において、電極17と20間の第１電子伝達蛋白質膜
18が介在しているが、第１電子伝達蛋白質膜18だけであ
れば、誘電体として作用するので両電極17と20間の絶縁
は保たれる。しかし、上記のように第1,第２及び第３電
子伝達蛋白質膜が配向を整えられて累積され、接着接合
されると、電極17と22間の電子の授受が可能となる。即
ち、電極20は第２電子伝達蛋白質膜19に対して絶縁的で
あるが、この電極20に電圧を印加することにより、第２
電子伝達蛋白質膜19に対して電圧的影響を与えることが
できる。即ち電極20は従来のFETのゲート電極に相当
し、電極17,22はそれぞれソース電極，ドレイン電極に
相当する。In FIG. 1, the first electron transfer protein membrane between electrodes 17 and 20
Although 18 is interposed, only the first electron transfer protein film 18 acts as a dielectric, so that insulation between both electrodes 17 and 20 is maintained. However, as described above, when the first, second and third electron transfer protein films are aligned, accumulated, and adhesively bonded, electrons can be transferred between the electrodes 17 and 22. That is, the electrode 20 is insulative to the second electron transfer protein film 19, but by applying a voltage to this electrode 20,
A voltage effect can be exerted on the electron transfer protein film 19. That is, the electrode 20 corresponds to the gate electrode of the conventional FET, and the electrodes 17 and 22 correspond to the source electrode and the drain electrode, respectively.
第３図（ａ）は本実施例のトランジスタ素子の電圧印加
状態を示す模式図で、同図（ｂ）はこのときの各電子伝
達蛋白質膜のレドックス電位状態を示す図である。電極
17と20との間に電極17側を正として電圧V1を印加し、電
極20と22との間に電極20側を正として電圧V2を印加する
と、レドックス電位状態は第３図（ｂ）の実線のように
変化する。同図の破線は電圧印加前の状態を示してお
り、V0は第１電子伝達蛋白質と第２電子伝達蛋白質との
レドックス電位の差である。FIG. 3 (a) is a schematic diagram showing the voltage application state of the transistor element of this example, and FIG. 3 (b) is a diagram showing the redox potential state of each electron transfer protein membrane at this time. electrode
When the voltage V 1 is applied between the electrodes 17 and 20 with the electrode 17 side being positive and the voltage V 2 is applied between the electrodes 20 and 22 with the electrode 20 side being positive, the redox potential state is shown in FIG. ) Changes like the solid line. The broken line in the figure shows the state before voltage application, and V 0 is the difference in redox potential between the first electron transfer protein and the second electron transfer protein.
このような本実施例の構成及び電圧印加に対応するレド
ックス電位の変化は、従来の半導体スイッチ素子（ｐ−
ｎ−ｐ接合タイプ）と同様と考えられ、上記構成により
スイッチ素子を分子レベルの超微細な大きさの素子とし
て実現でき、該素子を用いて高密度化，高速度化が可能
な集積回路が得られる。The change in the redox potential corresponding to the configuration and voltage application of the present embodiment is caused by the conventional semiconductor switch element (p-
It is considered to be similar to the np junction type), and with the above configuration, a switching element can be realized as an element having an ultrafine size at a molecular level, and an integrated circuit capable of achieving high density and high speed using the element is provided. can get.
また、上記実施例において電極と電子伝達蛋白質膜との
間に脂肪酸等の有機薄膜を形成した場合、該薄膜の有機
分子は蛋白質分子の支えとなり、電子伝達蛋白質の配向
が整えられる。これを第４図の模式図を用いてモデル的
に説明すると、有機薄膜23,24を設けることにより、該
膜の有機分子の凸部23aと第１の改変電子伝達蛋白質の
凹部18aがはまりあい、また第３の改変電子伝達蛋白質
の凹部21aと有機分子の凸部24aがはまりあい、これによ
り、第1,第３の改変電子伝達蛋白質の配向が整えられる
ことになる。また電極と電子伝達蛋白質とを直接接合さ
せると、それらの間の電子の授受が困難となったり、蛋
白質が変性してしまうことがあるが、上記有機薄膜を設
けることにより上記不具合は解消され、信頼性の高い素
子を形成できる。When an organic thin film of fatty acid or the like is formed between the electrode and the electron transfer protein film in the above example, the organic molecules of the thin film serve as a support for the protein molecule, and the orientation of the electron transfer protein is adjusted. This will be described as a model using the schematic diagram of FIG. 4. By providing the organic thin films 23 and 24, the convex portion 23a of the organic molecule of the membrane and the concave portion 18a of the first modified electron transfer protein fit together. Further, the concave portion 21a of the third modified electron transfer protein and the convex portion 24a of the organic molecule fit into each other, whereby the orientations of the first and third modified electron transfer proteins are adjusted. Further, when the electrode and the electron transfer protein are directly bonded, it may be difficult to transfer electrons between them or the protein may be denatured, but by providing the organic thin film, the above problem is solved, A highly reliable element can be formed.
なお、上記実施例では改変電子伝達蛋白質として、チト
クロームｃ等の天然電子伝達蛋白質にアミノ酸等を結合
したものを用いたが、これは上記天然電子伝達蛋白質の
活性中心の構造のみを保持してその他の部分を改変して
構成した改変蛋白質を用いてもよい。また第１〜第３電
子伝達物質の全てを改変電子伝達蛋白質で構成する必要
はない。In the above Examples, the modified electron transfer protein used was a natural electron transfer protein such as cytochrome c to which an amino acid or the like was bound. However, this modified electron transfer protein retains only the structure of the active center of the natural electron transfer protein. You may use the modified protein which comprised and modified the part of. Further, it is not necessary to compose all of the first to third electron transfer substances with the modified electron transfer protein.
また、電子伝達蛋白質への電子の供給に酵素を利用する
ようにしてもよい。In addition, an enzyme may be used to supply electrons to the electron transfer protein.
また、改変すべき天然の電子伝達蛋白質としては、非ヘ
ム−鉄・硫黄蛋白質、チトクロームｃ系蛋白質、チトク
ロームｂ系蛋白質、チトクロームａ、フラボドキシン、
プラストシアニン、チオレドキシンなどがある。The natural electron transfer proteins to be modified include non-heme-iron / sulfur proteins, cytochrome c-based proteins, cytochrome b-based proteins, cytochrome a, flavodoxin,
Examples include plastocyanin and thioredoxin.
また、各電子伝達物質は、異種電子伝達物質間では一定
方向のみに電子が流れるという性質を利用して累積膜に
垂直な方向には電子が流れ、上記累積膜に平行な方向で
隣接する電子伝達蛋白質分子間では電子の授受が起こら
ないような所定の分子配置をとるようLB法などで配向さ
せることが望ましい。Further, each electron transfer substance utilizes the property that electrons flow only in a fixed direction between different electron transfer substances, so that electrons flow in a direction perpendicular to the accumulation film and electrons adjacent to each other in the direction parallel to the accumulation film. It is desirable to orient by the LB method or the like so as to have a predetermined molecular arrangement so that transfer of electrons does not occur between transfer protein molecules.
さらに、上記実施例では２種類の電子伝達蛋白質の累積
膜でスイッチ素子を構成した場合を説明したが、これは
３種類以上の電子伝達蛋白質の累積膜として構成しても
よく、上記実施例と同様の効果を奏する。Further, in the above-mentioned embodiment, the case where the switch element is composed of the cumulative membranes of two kinds of electron transfer proteins has been described, but this may be constituted as a cumulative membrane of three or more kinds of electron transfer proteins. Has the same effect.
次に本願の第２の発明の実施例について説明する。Next, an embodiment of the second invention of the present application will be described.
前記第１の発明では、素子を構成する材料として、天然
の蛋白質の一部を改変したり、また天然の蛋白質にアミ
ノ酸等を化学的に結合したものを使用したが、本願の第
２の発明は、人工的な有機合成法により電子伝達蛋白質
の機能を模倣した有機分子あるいは有機金属錯体分子を
上記素子を構成する材料として用いたものである。In the first invention, as a material constituting the element, a part of a natural protein is modified, or a natural protein chemically bound with an amino acid or the like is used. However, the second invention of the present application Are those in which an organic molecule or an organometallic complex molecule that mimics the function of an electron transfer protein by an artificial organic synthetic method is used as a material constituting the above device.
上記のような電子伝達物質の例としては、Fe2+やフラビ
ンなど酸化還元反応をする化学物質が、化学的に合成し
たポリエチレン等のポリマーに取り囲まれるように形成
された人工電子伝達物質、即ちポリマー，ベンゼンなど
π電子を持つ物質，及び酸化還元物質を結合して形成さ
れた人工電子伝達物質がある。As an example of the electron transfer substance as described above, a chemical substance that undergoes a redox reaction such as Fe 2+ or flavin, an artificial electron transfer substance formed so as to be surrounded by a polymer such as chemically synthesized polyethylene, that is, There are polymers, substances having π electrons such as benzene, and artificial electron transfer substances formed by combining redox substances.
このようなものの構成及び作用効果は、前記第１の発明
の実施例と同様であり、素子サイズを生体分子レベルの
超微細な大きさに近づけることで可能である。The structure and operational effects of such a device are similar to those of the first embodiment of the present invention, and can be achieved by bringing the device size close to an ultrafine size at the biomolecule level.
以上のように、この発明によれば、相互にレドックス電
位の異なる電子伝達物質で第1,第2,第３の電子伝達物質
膜を形成し、各電子伝達物質のレドックス電位の違いを
利用してトランジスタ動作又はスイッチング動作を行わ
せるようにしたので、スイッチ素子サイズを生体分子レ
ベルの超微細な大きさに近づけることができ、該素子を
用いた集積回路の高密度，高速化を図ることができる効
果がある。As described above, according to the present invention, the first, second, and third electron mediator films are formed of electron mediators having different redox potentials, and the difference in redox potential of each electron mediator is utilized. Since the transistor operation or the switching operation is performed by using the switch element size, the switch element size can be made close to an ultrafine size at the biomolecule level, and an integrated circuit using the element can be increased in density and speed. There is an effect that can be done.
第１図は本発明の一実施例によるスイッチ素子が組み込
まれた装置の模式的断面構成図、第２図は該装置の分解
斜視図、第３図（ａ）は上記スイッチ素子の電圧印加状
態を示す模式図、第３図（ｂ）はその各電子伝達蛋白質
膜のレドックス電位状態を示す図、第４図は上記スイッ
チ素子中に形成された有機薄膜の作用効果を説明するた
めの模式図、第５図（ａ）は電子伝達蛋白質複合体の模
式図、第５図（ｂ）はそのレドックス電位を示す図、第
６図はミトコンドリアの内膜の電子伝達系を示す模式
図、第７図は従来の電界効果型トランジスタ素子を示す
断面図である。 17,20,22……電極、18……第１電子伝達蛋白質膜、19…
…第２電子伝達蛋白質膜、21……第３電子伝達蛋白質
膜。 なお図中同一符号は同一又は相当部分を示す。FIG. 1 is a schematic cross-sectional configuration diagram of an apparatus incorporating a switch element according to an embodiment of the present invention, FIG. 2 is an exploded perspective view of the apparatus, and FIG. 3 (a) is a voltage application state of the switch element. Fig. 3 (b) is a diagram showing the redox potential state of each electron transfer protein membrane, and Fig. 4 is a schematic diagram for explaining the action and effect of the organic thin film formed in the switch element. FIG. 5 (a) is a schematic diagram of an electron transfer protein complex, FIG. 5 (b) is a diagram showing its redox potential, FIG. 6 is a schematic diagram showing an electron transport system of the inner membrane of mitochondria, FIG. The figure is a cross-sectional view showing a conventional field effect transistor element. 17,20,22 ... Electrodes, 18 ... First electron transfer protein membrane, 19 ...
… Second electron transfer protein membrane, 21 …… Third electron transfer protein membrane. The same reference numerals in the drawings indicate the same or corresponding parts.
───────────────────────────────────────────────────── フロントページの続き (72)発明者 川窪 広明 兵庫県尼崎市塚口本町８丁目１番１号 三 菱電機株式会社中央研究所内 (56)参考文献 特開 昭61−163663（ＪＰ，Ａ) ─────────────────────────────────────────────────── ─── Continuation of the front page (72) Hiroaki Kawakubo 8-1-1 Tsukaguchi Honcho, Amagasaki City, Hyogo Prefecture Inside the Central Research Laboratory, Sanryo Electric Co., Ltd. (56) Reference JP-A-61-163663 (JP, A)
Claims (13)
を一定方向に伝達可能な第１の電子伝達物質で作成され
た第１電子伝達物質膜と、 上記第１の電子伝達物質のレドックス電位と異なるレド
ックス電位を有する第２の電子伝達物質で作成され、上
記第１電子伝達物質膜上に累積して接着接合された第２
電子伝達物質膜と、 上記第２の電子伝達物質と異なるレドックス電位を有す
る第３の電子伝達物質で作成され、上記第２電子伝達物
質膜上に累積して接着接合された第３電子伝達物質膜
と、 それぞれ上記第1,第2,第３の電子伝達物質に接続された
第1,第2,第３の電極とを備え、 上記第１ないし第３の電子伝達物質のうちの少なくとも
１つは天然に存在する電子伝達蛋白質にアミノ酸又はア
ミノ酸誘導体を結合してなるものであり、上記第1,第2,
第３の電子伝達物質のレドックス電位の違いを利用して
トランジスタ特性又はスイッチング特性を呈するように
したことを特徴とするスイッチ素子。1. A first electron mediator film made of a first electron mediator, which is a biomaterial or a pseudo-biomaterial and can transfer electrons in a certain direction, and a redox potential of the first electron mediator. A second electron transfer material having a different redox potential, accumulated on the first electron transfer material film and adhesively bonded to the second electron transfer material film.
A third electron transfer material made of an electron transfer material film and a third electron transfer material having a redox potential different from that of the second electron transfer material, and accumulated and bonded on the second electron transfer material film. A film, and first, second, and third electrodes respectively connected to the first, second, and third electron transfer materials, and at least one of the first to third electron transfer materials Is a naturally-occurring electron transfer protein to which an amino acid or an amino acid derivative is bound.
A switch element characterized by exhibiting transistor characteristics or switching characteristics by utilizing a difference in redox potential of a third electron transfer substance.
3に、あるいはＣをSiに置換してなるものであることを
特徴とする特許請求の範囲第１項記載のスイッチ素子。2. The above amino acid derivative, wherein H is F or CH
The switch element according to claim 1, wherein the switch element is formed by replacing 3 or C by Si.
ヘム−鉄・硫黄蛋白質，チトクロームｃ系蛋白質，チト
クロームｂ系蛋白質，チトクロームa,フラボドキシン，
プラストシアニン，又はチオレドキシンであることを特
徴とする特許請求の範囲第１項又は第２項記載のスイッ
チ素子。3. The naturally-occurring electron transfer proteins include non-heme-iron / sulfur proteins, cytochrome c type proteins, cytochrome b type proteins, cytochrome a, flavodoxin,
The switch element according to claim 1, which is plastocyanin or thioredoxin.
を特徴とする特許請求の範囲第１項ないし第３項のいず
れか記載のスイッチ素子。4. The switch element according to claim 1, wherein the electron transfer substance film is a monomolecular film.
利用するようにしたことを特徴とする特許請求の範囲第
１項ないし第４項のいずれかに記載のスイッチ素子。5. The switch element according to any one of claims 1 to 4, wherein an enzyme is used to supply electrons to the electron transfer substance.
する特許請求の範囲第１項ないし第５項のいずれかに記
載のスイッチ素子。6. The switch element according to claim 1, wherein each of the electrodes is a metal electrode.
修飾したものであることを特徴とする特許請求の範囲第
６項記載のスイッチ素子。7. The switch element according to claim 6, wherein each of the electrodes is a metal electrode chemically modified with an organic molecule.
質が、各膜が累積された方向である膜面に垂直な方向に
電子が流れ、水平方向の隣接する電子伝達物質分子間で
は電子の授受がなされないよう配向されていることを特
徴とする特許請求の範囲第１項ないし第７項のいずれか
に記載のスイッチ素子。8. The electron transfer material film of each of the electron transfer materials has electrons flowing in a direction perpendicular to a film surface, which is a direction in which the respective films are accumulated, and between adjacent electron transfer material molecules in a horizontal direction. The switch element according to any one of claims 1 to 7, wherein the switch element is oriented so that electrons are not transferred.
脂質又は脂肪酸を用いたことを特徴とする特許請求の範
囲第１項ないし第８項のいずれかに記載のスイッチ素
子。9. A support for orienting the electron transfer material,
The switch element according to any one of claims 1 to 8, wherein a lipid or a fatty acid is used.
れらの間の電流の授受を良好なものとし、かつ上記電子
伝達物質を配向支持する有機分子又は有機金属錯体から
なる薄層が形成されていることを特徴とする特許請求の
範囲第１項記載のスイッチ素子。10. A thin layer made of an organic molecule or an organometallic complex for favorably exchanging an electric current between the electron-transporting substance and the electrode and for orientation-supporting the electron-transporting substance. The switch element according to claim 1, wherein the switch element is formed.
子を一定方向に伝達可能な第１の電子伝達物質で作成さ
れた第１電子伝達物質膜と、 上記第１の電子伝達物質のレドックス電位と異なるレド
ックス電位を有する第２の電子伝達物質で作成され、上
記第１電子伝達物質膜上に累積して接着接合された第２
電子伝達物質膜と、 上記第２の電子伝達物質のレドックス電位と異なるレド
ックス電位を有する第３の電子伝達物質で作成され、上
記第２電子伝達物質上に累積して接着接合された第３電
子伝達物質膜と、 それぞれ上記第1,第2,第３の電子伝達物質に接続された
第1,第2,第３の電極とを備え、 上記第１ないし第３の電子伝達物質のうちの少なくとも
１つは人工的な有機合成法により天然に存在する電子伝
達蛋白質の機能を模倣してなる有機分子又は有機金属錯
体分子であり、上記第1,第2,第３の電子伝達物質のレド
ックス電位の違いを利用してトランジスタ特性又はスイ
ッチング特性を呈するようにしたことを特徴とするスイ
ッチ素子。11. A first electron mediator film made of a first electron mediator, which is a biomaterial or a pseudo-biomaterial and can transfer electrons in a certain direction, and a redox potential of the first electron mediator. A second electron transfer material having a different redox potential, accumulated on the first electron transfer material film and adhesively bonded to the second electron transfer material film.
A third electron, which is made of an electron transfer substance film and a third electron transfer substance having a redox potential different from the redox potential of the second electron transfer substance, and is accumulated and adhesively bonded on the second electron transfer substance. Of the first to third electron transfer materials, the transfer material film and the first, second, and third electrodes respectively connected to the first, second, and third electron transfer materials are provided. At least one is an organic molecule or an organometallic complex molecule that mimics the function of a naturally-occurring electron transfer protein by an artificial organic synthetic method, and the redox of the above-mentioned first, second, and third electron transfer substances. A switching element characterized by exhibiting transistor characteristics or switching characteristics by utilizing a difference in potential.
酸化還元物質がポリマーに取り囲まれるようにして形成
されたものであることを特徴とする特許請求の範囲第11
項記載のスイッチ素子。12. The organic molecule or organometallic complex molecule,
11. The redox material according to claim 11, wherein the redox material is formed so as to be surrounded by a polymer.
The switch element according to the item.
ポリマー，π電子を持つ物質，及び酸化還元反応をする
物質を結合してなるものであることを特徴とする特許請
求の範囲第12項記載のスイッチ素子。13. The organic molecule or organometallic complex molecule,
13. The switch element according to claim 12, wherein the switch element comprises a polymer, a substance having π electrons, and a substance that undergoes a redox reaction.
Priority Applications (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61155450A JPH0770764B2 (en) | 1986-07-01 | 1986-07-01 | Switch element |
| US07/068,297 US4764415A (en) | 1986-07-01 | 1987-07-01 | Electric element using oxidation-reduction substances |
| DE19873721793 DE3721793A1 (en) | 1986-07-01 | 1987-07-01 | ELECTRICAL ELEMENT USING OXIDATION REDUCTION SUBSTANCES |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61155450A JPH0770764B2 (en) | 1986-07-01 | 1986-07-01 | Switch element |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6310565A JPS6310565A (en) | 1988-01-18 |
| JPH0770764B2 true JPH0770764B2 (en) | 1995-07-31 |
Family
ID=15606308
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP61155450A Expired - Lifetime JPH0770764B2 (en) | 1986-07-01 | 1986-07-01 | Switch element |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0770764B2 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2515684Y2 (en) * | 1991-06-18 | 1996-10-30 | 株式会社角田商店 | Magnet type stopper |
-
1986
- 1986-07-01 JP JP61155450A patent/JPH0770764B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6310565A (en) | 1988-01-18 |
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