ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Electrochemistry of the CuA domain of Thermus thermophilus cytochrome ba 3 (1996)
    Springer
    JBIC 1 (1996), S. 529-531 
    Details
    ISSN: 1432-1327
    Keywords: Key words CuA domain ; Thermus thermophilus ; Cytochrome ba3 ; Electrochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The electrochemistry of a water-soluble fragment from the CuA domain of Thermus thermophilus cytochrome ba 3 has been investigated. At 25  °C, CuA exhibits a reversible reduction at a pyridine-4-aldehydesemicarbazone-modified gold electrode (0.1 M Tris, pH 8) with E° = 0.24 V vs NHE. Thermodynamic parameters for the [Cu(Cys)2Cu]+/0 electrode reaction were determined by variable-temperature electrochemistry (ΔS°rc = –5.4(12) eu, ΔS° = –21.0(12) eu, ΔH° = –11.9(4) kcal/mol;ΔG° = –5.6 (11) kcal/mol). The relatively small reaction entropy is consistent with a low reorganization energy for [Cu(Cys)2Cu]+/0 electron transfer. An irreversible oxidation of [Cu(Cys)2Cu]+ at 1 V vs NHE confirms that the CuII:CuII state of CuA is significantly destabilized relative to the CuII state of analogous blue-copper proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050088
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Electron transfer in ruthenium-modified proteins (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 295-302 
    Details
    ISSN: 1573-6881
    Keywords: Electron transfer ; cytochromec ; azurin ; ruthenium ; electronic coupling ; driving-force dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Photochemical techniques have been used to measure the kinetics of intramolecular electron transfer in Ru(bpy)2(im)(His)2+-modified (bpy = 2,2′-bipyridine; im = imidazole) cytochromec and azurin. A driving-force study with the His33 derivatives of cytochromec indicates that the reorganization energy (γ) for Fe2+→Ru3+ ET reactions is 0.8 eV. Reductions of the ferriheme by either an excited complex,*Ru2+, or a reduced complex, Ru+, are anomalously fast and may involve formation of an electronically excited ferroheme. The distance dependence of Fe2+→Ru3+ and Cu+→Ru3+ electron transfer in 12 different Ru-modified cytochromes and azurins has been analyzed using a tunneling-pathway model. The ET rates in 10 of the 12 systems exhibit an exponential dependence on metal-metal separation (decay constant of 1.06 å−1) that is consistent with predictions of the pathway model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110099
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...