@article{BistolasChristensonRuzgasetal.2004,
  author    = {Bistolas, Nikitas and Christenson, A. and Ruzgas, T. and Jung, Christiane and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Spectroelectrochemistry of cytochrome P450cam},
  year      = {2004},
  abstract  = {The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved},
  language  = {en}
}
@article{BistolasWollenbergerJungetal.2005,
  author    = {Bistolas, Nikitas and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Cytochrome P450 biosensors : a review},
  year      = {2005},
  abstract  = {Cytochrome P450 (CYP) is a large family of enzymes containing heme as the active site. Since their discovery and the elucidation of their structure, they have attracted the interest of scientist for many years, particularly due to their catalytic abilities. Since the late 1970s attempts have concentrated on the construction and development of electrochemical sensors. Although sensors based on mediated electron transfer have also been constructed, the direct electron transfer approach has attracted most of the interest. This has enabled the investigation of the electrochemical properties of the various isoforms of CYP. Furthermore, CYP utilized to construct biosensors for the determination of substrates important in environmental monitoring, pharmaceutical industry and clinical practice. (c) 2004 Elsevier B. V. All rights reserved},
  language  = {en}
}
@article{FreibergMoronaVandenBoschetal.2003,
  author    = {Freiberg, Alexander and Morona, Renato and Van den Bosch, Luisa and Jung, Christiane and Behlke, Joachim and Carlin, Nung and Seckler, Robert and Baxa, Ulrich},
  title     = {The tailspike protein of Shigella phage Sf6 : a structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain},
  issn      = {0021-9258},
  year      = {2003},
  abstract  = {Bacteriophage Sf6 tailspike protein is functionally equivalent to the well characterized tailspike ofSalmonella phage P22, mediating attachment of the viral particle to host cell-surface polysaccharide. However, there is significant sequence similarity between the two 70-kDa polypeptides only in the N-terminal putative capsid-binding domains. The major, central part of P22 tailspike protein, which forms a parallel ;-helix and is responsible for saccharide binding and hydrolysis, lacks detectable sequence homology to the Sf6 protein. After recombinant expression in Escherichia coli as a soluble protein, the Sf6 protein was purified to homogeneity. As shown by circular dichroism and Fourier transform infrared spectroscopy, the secondary structure contents of Sf6 and P22 tailspike proteins are very similar. Both tailspikes are thermostable homotrimers and resist denaturation by SDS at room temperature. The specific endorhamnosidase activities of Sf6 tailspike protein toward fluorescence-labeled dodeca-, deca-, and octasaccharide fragments of Shigella O-antigen suggest a similar active site topology of both proteins. Upon deletion of the N-terminal putative capsid-binding domain, the protein still forms a thermostable, SDS-resistant trimer that has been crystallized. The observations strongly suggest that the tailspike of phage Sf6 is a trimeric parallel ;-helix protein with high structural similarity to its functional homolog from phage P22.},
  language  = {en}
}
@phdthesis{Jung1998,
  author    = {Jung, Christiane},
  title     = {Strukturdynamik und Konformationssubzust{\"a}nde in Proteinen : das Enzym Cytochrom P450},
  pages     = {79 S., Seite A 1 - A 174, 2 Bl. : graph. Darst.},
  year      = {1998},
  language  = {de}
}
@article{JungPfeilKoepkeetal.1994,
  author    = {Jung, Christiane and Pfeil, Wolfgang and K{\"o}pke, Karla and Schulze, Heike and Ristau, Otto},
  title     = {Conformational states and substates of cytochrome P450cam - insight in protein dynamics and folding},
  year      = {1994},
  language  = {en}
}
@article{LeiWollenbergerJungetal.2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Clay-bridged electron transfer between cytochrome P450(cam) and electrode},
  year      = {2000},
  language  = {en}
}
@article{PfeilNoeltingJung1993,
  author    = {Pfeil, Wolfgang and N{\"o}lting, Bengt and Jung, Christiane},
  title     = {Apocytochrome P450cam is a native protein with some intermediate-like properties},
  year      = {1993},
  language  = {en}
}
@article{PfeilNoeltingJung1993,
  author    = {Pfeil, Wolfgang and N{\"o}lting, Bengt and Jung, Christiane},
  title     = {Thermodynmic properties of apocytochrome P450cam},
  year      = {1993},
  language  = {en}
}
@article{WollenbergerBistolasJungetal.2004,
  author    = {Wollenberger, Ursula and Bistolas, Nikitas and Jung, Christiane and Shumyantseva, V. V. and Ruzgas, T. and Scheller, Frieder W.},
  title     = {Elektroden-Design f{\"u}r elektronische Wechselwirkung mit Monooxygenasen},
  isbn      = {3-8047-2132-x},
  year      = {2004},
  language  = {de}
}
@article{WollenbergerJung2001,
  author    = {Wollenberger, Ursula and Jung, Christiane},
  title     = {Cytochrom P450-Elektrochemie},
  year      = {2001},
  language  = {de}
}