Remote activation of nanoparticulate biomimetic activity by light triggered pH-jump

2018 ◽  
Vol 54 (62) ◽  
pp. 8641-8644 ◽  
Author(s):  
Xiaopei Wang ◽  
Ao Gong ◽  
Wenhao Luo ◽  
Haiqing Wang ◽  
Changxu Lin ◽  
...  

By incorporating flash photolysis reagents, a facile and versatile method for the photo-regulation of pH-dependent activities of artificial enzymes is presented.

1991 ◽  
Vol 276 (1) ◽  
pp. 121-124
Author(s):  
A J Mathews ◽  
T Brittain

The reactivity of carbodi-imide-modified tuna and horse heart cytochromes c with the ferrous ion ligands CO and O2 has been studied. Both modified cytochromes bind one molecule of CO. Stopped-flow and flash-photolysis experiments indicate the presence of three kinetic processes in the reaction of the cytochromes with CO. The second-order rate constants associated with all three kinetic process are pH-independent being 2.8 x 10(5) M-1.s-1, 3.8 x 10(4) M-1.s-1 and 4 x 10(3) M-1.s-1 under all conditions studied. The concentration-dependence of the contributions made by each of the processes to the overall absorbance change indicates that the fast and slow kinetic phases are associated with two forms of the cytochromes which are in equilibrium, whereas the intermediate phase arises from a separate cytochrome species. The quantum yield for the photodissociation of CO from the ferrous cytochromes is unusually low. Both modified cytochromes are capable of binding and reducing O2. In the presence of excess reductant, the modified cytochromes can catalytically reduce large molar excesses of O2. In the absence of excess reducing agent, the oxy complex initially formed undergoes a pH-dependent intramolecular electron-transfer process with half-life approx. 10 min. EDC [1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide]-promoted internal cross-linking is proposed to account for differences between the EDC-modified proteins and carboxymethylated cytochrome c.


1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.


2002 ◽  
Vol 76 (5) ◽  
pp. 480 ◽  
Author(s):  
Xavier Damoiseau ◽  
Francis Tfibel ◽  
Maryse Hoebeke ◽  
Marie-Pierre Fontaine-Aupart

2000 ◽  
Vol 72 (4) ◽  
pp. 451 ◽  
Author(s):  
M. Bazin ◽  
F. Bosca ◽  
M. L. Marin ◽  
M. A. Miranda ◽  
L. K. Patterson ◽  
...  

1999 ◽  
Vol 70 (3) ◽  
pp. 292
Author(s):  
Ann Cantrell ◽  
David J. McGarvey ◽  
Louise Mulroy ◽  
T. George Truscott

2018 ◽  
Author(s):  
Fei He ◽  
Li Mi ◽  
Yanfei Shen ◽  
Toshiyuki Mori ◽  
Songqin Liu ◽  
...  

Developing highly efficient artificial enzymes that directly employ O<sub>2</sub> as terminal oxidant has long been pursued but has rarely achieved yet. We report Fe-N-C has unusual enzyme-like activity in both dehydrogenation and monoxygenation of organic substrates with ~100% selectivity by direct using O<sub>2</sub>.


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