Photoactivation Studies of Zinc Porphyrin-Myoglobin System and Its Application for Light-Chemical Energy Conversion

被引:5
作者
Chang, Chin-Hao [1 ]
Hu, Yi-Ting [1 ]
Lo, Chen-Fu [2 ]
Luo, Liyang [3 ,4 ]
Lin, Hung-Ming [1 ]
Chang, Cheng-Hsiang [1 ]
Lin, Ching-Yao [2 ]
Diau, Eric Wei-Guang [3 ,4 ]
Wu, Tung-Kung [1 ]
机构
[1] Natl Chiao Tung Univ, Dept Biol Sci & Technol, Hsinchu 30068, Taiwan
[2] Natl Chi Nan Univ, Dept Appl Chem, Puli, Nantou County, Taiwan
[3] Natl Chiao Tung Univ, Dept Appl Chem, Hsinchu 30068, Taiwan
[4] Natl Chiao Tung Univ, Inst Mol Sci, Hsinchu 30068, Taiwan
来源
INTERNATIONAL JOURNAL OF BIOLOGICAL SCIENCES | 2011年 / 7卷 / 08期
关键词
photoelectrochemical energy conversion; zinc protoporphyrin; myoglobin; oxidoredox reaction; biosensitizer; NICOTINAMIDE ADENINE-DINUCLEOTIDE; ELECTRON-TRANSFER; TRIPLET-STATE; CYTOCHROME-C; SOLAR-CELLS; RECONSTITUTED MYOGLOBIN; REDUCTION; DIMERS; OXIDATION; HYDROGEN;
D O I
10.7150/ijbs.7.1203
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
An artificial zinc porphyrin-myoglobin- based photo-chemical energy conversion system, consisting of ZnPP-Mb or ZnPE1-Mb as a photosensitizer, NADP(+) as an electron acceptor, and triethanolamine as an electron donor, has been constructed to mimic photosystem I. The photoirradiated product is able to reduce a single-electron acceptor protein cytochrome c, but cannot catalyze the two-electron reduction of acetaldehyde by alcohol dehydrogenase, thus demonstrating a single electron transfer mechanism. Furthermore, the artificial system can bifunctionally promote oxidoredox reactions, depending on the presence or absence of a sacrificial electron donor, thus suggesting its potential application in electrochemical regeneration steps involved in chemical transformation and/or energy conversion.
引用
收藏
页码:1203 / 1213
页数:11
相关论文
共 62 条
[51]  
Nishiyama K, 1999, CHEM LETT, P357
[52]   Triplet state magnetic resonance and fluorescence spectroscopy of metal-substituted hemoglobins [J].
Polm, MW ;
Schaafsma, TJ .
BIOPHYSICAL JOURNAL, 1997, 72 (01) :373-382
[53]   Study of NADH stability using ultraviolet-visible spectrophotometric analysis and factorial design [J].
Rover, L ;
Fernandes, JCB ;
Neto, GD ;
Kubota, LT ;
Katekawa, E ;
Serrano, SHP .
ANALYTICAL BIOCHEMISTRY, 1998, 260 (01) :50-55
[54]  
Shelnutt JA, 1990, PHOTOCHEMICAL DRIVEN, V437
[55]   Reductive quenching of the triplet state of zinc cytochrome c by the hexacyanoferrate(II) anion and by conjugate bases of ethylenediaminetetraacetic acid [J].
Shen, CY ;
Kostic, NM .
INORGANIC CHEMISTRY, 1996, 35 (10) :2780-2784
[56]   The electronic structure of transient species in the photochemical reduction of porphyrins [J].
Sinyakov, GN ;
Shul'ga, AM ;
Filatov, IV ;
Dzilinsky, K .
HIGH ENERGY CHEMISTRY, 2002, 36 (04) :255-259
[57]   CLEAVAGE OF THE HAEM-PROTEIN LINK BY ACID METHYLETHYLKETONE [J].
TEALE, FWJ .
BIOCHIMICA ET BIOPHYSICA ACTA, 1959, 35 (02) :543-543
[58]   Intracomplex quenching by copper(II) ion of excited singlet and triplet states of zinc myoglobin modified with diethylenetriaminepentaacetic acid [J].
Tsukahara, K ;
Kimura, C ;
Sakurai, T .
CHEMISTRY LETTERS, 1997, (07) :601-602
[59]  
Martínez-Díaz MV, 2010, HANDB PORPHYR SCI, V10, P141
[60]  
WU JT, 1986, CLIN CHEM, V32, P314