Abstract
To make a single molecular photo-device, it is essential to control the exact orientation of two types of proteins. We made a chimeric protein in which cytochrome b562 was linked to the N-terminus of enhanced green fluorescent protein, cytb562-EGFP. Within cytb562-EGFP, the excitation energy of EGFP was transferred to the cytochrome b562 cofactor fixed proximally to EGFP. Cytb562-EGFP was engineered so that iron protoporphyrin IX was substituted by zinc protoporphyrin IX to make it a suitable cofactor for photo-induced electron transfer. The photosensitizer pigment was optimized and the EGFP was replaced by a blue fluorescent mutant that gave 15% higher energy transfer efficiency.
| Original language | English |
|---|---|
| Pages (from-to) | 121-125 |
| Number of pages | 5 |
| Journal | Biotechnology Letters |
| Volume | 26 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jan 2004 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
Cite this
Rational design of a protein-based molecular device consisting of blue fluorescent protein and zinc protoporphyrin IX incorporated into a cytochrome b562 scaffold. / Takeda, Shuji; Kamiya, Noriho; Nagamune, Teruyuki.
In: Biotechnology Letters, Vol. 26, No. 2, 01.2004, p. 121-125.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Rational design of a protein-based molecular device consisting of blue fluorescent protein and zinc protoporphyrin IX incorporated into a cytochrome b562 scaffold
AU - Takeda, Shuji
AU - Kamiya, Noriho
AU - Nagamune, Teruyuki
PY - 2004/1
Y1 - 2004/1
N2 - To make a single molecular photo-device, it is essential to control the exact orientation of two types of proteins. We made a chimeric protein in which cytochrome b562 was linked to the N-terminus of enhanced green fluorescent protein, cytb562-EGFP. Within cytb562-EGFP, the excitation energy of EGFP was transferred to the cytochrome b562 cofactor fixed proximally to EGFP. Cytb562-EGFP was engineered so that iron protoporphyrin IX was substituted by zinc protoporphyrin IX to make it a suitable cofactor for photo-induced electron transfer. The photosensitizer pigment was optimized and the EGFP was replaced by a blue fluorescent mutant that gave 15% higher energy transfer efficiency.
AB - To make a single molecular photo-device, it is essential to control the exact orientation of two types of proteins. We made a chimeric protein in which cytochrome b562 was linked to the N-terminus of enhanced green fluorescent protein, cytb562-EGFP. Within cytb562-EGFP, the excitation energy of EGFP was transferred to the cytochrome b562 cofactor fixed proximally to EGFP. Cytb562-EGFP was engineered so that iron protoporphyrin IX was substituted by zinc protoporphyrin IX to make it a suitable cofactor for photo-induced electron transfer. The photosensitizer pigment was optimized and the EGFP was replaced by a blue fluorescent mutant that gave 15% higher energy transfer efficiency.
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UR - http://www.scopus.com/inward/citedby.url?scp=1042268320&partnerID=8YFLogxK
U2 - 10.1023/B:BILE.0000012889.24412.ca
DO - 10.1023/B:BILE.0000012889.24412.ca
M3 - Article
C2 - 15000478
AN - SCOPUS:1042268320
VL - 26
SP - 121
EP - 125
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 2
ER -