Bell-shaped dependence of the rate of ultrafast photoinduced electron transfer from aromatic amino acids to the excited flavin on the donor–acceptor distance in FMN binding proteins

2014 ◽  
Vol 1030 ◽  
pp. 9-16 ◽  
Author(s):  
Nadtanet Nunthaboot ◽  
Kiattisak Lugsanangarm ◽  
Somsak Pianwanit ◽  
Sirirat Kokpol ◽  
Fumio Tanaka ◽  
...  
2015 ◽  
Vol 17 (26) ◽  
pp. 16813-16825 ◽  
Author(s):  
Fumio Tanaka ◽  
Kiattisak Lugsanangarm ◽  
Nadtanet Nunthaboot ◽  
Arthit Nueangaudom ◽  
Somsak Pianwanit ◽  
...  

Emission wavelength-dependence of the relationship between logarithmic ET rate vs. donor–acceptor distance in pyranose 2-oxidase.


10.5772/38078 ◽  
2012 ◽  
Author(s):  
Kiattisak Lugsanangarm ◽  
Nadtanet Nunthaboot ◽  
Somsak Pianwanit ◽  
Sirirat Kokpol ◽  
Fumio Tanak

2005 ◽  
Vol 3 (5) ◽  
pp. 881 ◽  
Author(s):  
Nikolai E. Polyakov ◽  
Vladimir K. Khan ◽  
Marc B. Taraban ◽  
Tatyana V. Leshina ◽  
Olga A. Luzina ◽  
...  

2014 ◽  
Vol 18 (10n11) ◽  
pp. 982-990 ◽  
Author(s):  
Kei Ohkubo ◽  
Yuki Kawashima ◽  
Kentaro Mase ◽  
Hayato Sakai ◽  
Taku Hasobe ◽  
...  

An electron donor–acceptor supramolecular complex was formed between an anionic zinc chlorin carboxylate ( ZnCh -) and lithium-ion-encapsulated [60]fullerene ( Li +@ C 60) by an electrostatic interaction in benzonitrile ( PhCN ). Photoinduced electron transfer in the supramolecular complex of ZnCh -/ Li +@ C 60 resulted in the formation of the charge-separated state via electron transfer from the triplet excited state of ZnCh - to Li +@ C 60. We report herein photovoltaic cells using ZnCh -/ Li +@ C 60 nanoclusters, which are assembled on the optically transparent electrode (OTE) of nanostructured SnO 2 (OTE/ SnO 2). The photoelectrochemical behavior of the nanostructured SnO 2 film of supramolecular nanoclusters of ZnCh - and Li +@ C 60 denoted as OTE/ SnO 2/( ZnCh -/ Li +@ C 60)n is significantly higher than the single component films of ZnCh - or Li +@ C 60 clusters, denoted as OTE/ SnO 2/( ZnCh -)n or OTE/ SnO 2/( Li +@ C 60)n.


1975 ◽  
Vol 19 (1) ◽  
pp. 203-213
Author(s):  
W.B. Amos ◽  
L.M. Routledge ◽  
F.F. Yew

The proteins of the contractile spasmoneme of Zoothamnium have been examined for comparison with other motile systems. Though capable of calcium-induced contraction, glycerinated preparations of the spasmoneme contain neither actin nor tubulin at levels that can be detected in polyacrylamide gels. Sixty per cent of the protein in sodium dodecyl sulphate gels migrates in a band at a molecular weight of approximately 20,000, consisting largely of 2 similar protein species which are here given the name of spasmins. The amino acid composition of 2 spasmin fractions has been determined by a fluorimetric method. They are rich in Asx, Glx and serine, but have few aromatic amino acids and no cystine or methionine. In calcium-buffered polyacrylamide gels, it was observed that a reduction in the electrophoretic mobility of the spasmins was induced specifically by calcium (but not magnesium) at the same low concentrations as induce contraction. This indicates that the spasmins are calcium-binding proteins which may be involved directly in the calcium-induced contraction of the spasmoneme.


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