Results 281 to 290 of about 203,240 (311)
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Biochemistry, 2016
To understand how a protein folds and behaves inside living cells, the effects of synthetic crowding media on protein folding, function, stability, and association have been studied in detail. Because the effect of excluded volume is more prominent in an
S. Paul+4 more
semanticscholar +1 more source
To understand how a protein folds and behaves inside living cells, the effects of synthetic crowding media on protein folding, function, stability, and association have been studied in detail. Because the effect of excluded volume is more prominent in an
S. Paul+4 more
semanticscholar +1 more source
Chemical Communications, 2016
Ionic liquid (IL) surfactant choline dioctylsulfosuccinate, [Cho][AOT], formed polydispersed vesicular structures in the IL, ethylmethylimidazolium ethylsulfate, [C2mim][C2OSO3].
Pankaj Bharmoria, Arvind Kumar
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Ionic liquid (IL) surfactant choline dioctylsulfosuccinate, [Cho][AOT], formed polydispersed vesicular structures in the IL, ethylmethylimidazolium ethylsulfate, [C2mim][C2OSO3].
Pankaj Bharmoria, Arvind Kumar
semanticscholar +1 more source
Interactions of Cytochrome c Peroxidase with Lysine Peptides
Biochemical and Biophysical Research Communications, 2000Structural change of Cytochrome c peroxidase (CcP) due to interaction with lysine peptides (Lysptds) has been studied by absorption spectra and measurements on electron transfer between cytochrome c (cyt c) and CcP in the presence of Lysptd. Peaks were observed in the difference absorption spectrum of CcP between in the presence and absence of Lysptds,
Shun K. Hirota+3 more
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Physical Chemistry, Chemical Physics - PCCP, 2015
Choline dioctylsulfosuccinate [Cho][AOT] (a surface active ionic liquid) has been found to induce all-α to α + β conformational transition in the secondary structure of enzyme cytochrome c (Cyt c) with an enhanced peroxidase activity in its aqueous ...
Pankaj Bharmoria+4 more
semanticscholar +1 more source
Choline dioctylsulfosuccinate [Cho][AOT] (a surface active ionic liquid) has been found to induce all-α to α + β conformational transition in the secondary structure of enzyme cytochrome c (Cyt c) with an enhanced peroxidase activity in its aqueous ...
Pankaj Bharmoria+4 more
semanticscholar +1 more source
The cytochrome c peroxidase of Paracoccus denitrificans
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991The size, visible absorption spectra, nature of haem and haem content suggest that the cytochrome c peroxidase of Paracoccus denitrificans is related to that of Pseudomonas aeruginosa. However, the Paracoccus enzyme shows a preference for cytochrome c donors with a positively charged 'front surface' and in this respect resembles the cytochrome c ...
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The catalytic mechanism of Pseudomonas cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1981Abstract The catalytic mechanism of Pseudomonas cytochrome c peroxidase has been studied using rapid-scan spectrometry and stopped-flow measurements. The reaction of the totally ferric form of the enzyme with H 2 O 2 was slow and the complex formed was inactive in the peroxidatic cycle, whereas partially reduced enzyme formed highly reactive ...
Marjaana Rönnberg+3 more
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FEMS Microbiology Letters, 2014
A new rapid and simple method was developed for the detection of Escherichia coli by constructing a recombinant T4 phage carrying the cytochrome c peroxidase gene derived from Saccharomyces cerevisiae (T4ccp) using which, the colorimetric detection of E.
H. A. Hoang, Michiharu Abe, K. Nakasaki
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A new rapid and simple method was developed for the detection of Escherichia coli by constructing a recombinant T4 phage carrying the cytochrome c peroxidase gene derived from Saccharomyces cerevisiae (T4ccp) using which, the colorimetric detection of E.
H. A. Hoang, Michiharu Abe, K. Nakasaki
semanticscholar +1 more source
Cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy
Biochemistry, 1992Complex formation between ferricytochrome c peroxidase (CCP) and ferricytochrome c from yeast [cyt(Y)] and horse heart [cyt(H)] was studied by resonance Raman spectroscopy. On the basis of a detailed spectral analysis of the free proteins, it was possible to attribute changes in the spectra of the complexes to the individual proteins.
P. Hildebrandt+2 more
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Biochemistry, 1993
We have studied the affinity and stoichiometry of binding of cytochrome c (Cc) to zinc-substituted cytochrome c peroxidase [(ZnP)CcP], which is structurally and electrostatically equivalent to ferrous CcP. Transient absorption spectroscopy has been used to measure both the total quenching of the triplet-state (ZnP)CcP [3(ZnP)CcP] by Fe3+Cc and the ...
Brian M. Hoffman, Eric D. A. Stemp
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We have studied the affinity and stoichiometry of binding of cytochrome c (Cc) to zinc-substituted cytochrome c peroxidase [(ZnP)CcP], which is structurally and electrostatically equivalent to ferrous CcP. Transient absorption spectroscopy has been used to measure both the total quenching of the triplet-state (ZnP)CcP [3(ZnP)CcP] by Fe3+Cc and the ...
Brian M. Hoffman, Eric D. A. Stemp
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Investigation of Electron Tunneling Between Cytochrome c Peroxidase and Cytochrome c
Science, 1978The nature of electron transfer between the bound complex cytochrome c and cytochrome c peroxidase has been investigated. Experimental verification of the predicted charge-transfer band provides evidence of electron tunneling as the mechanism of transfer between these molecules in solution at room temperature.
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