Bioelectrochemical analysis of de novo designed proteins having different motifs binding iron-sulfur cluster and iron-porphyrins

• Autorzy: Lazicka M. , Grzyb J.
• Języki publikacji: EN
• Wydawca: -
• Czasopismo: Current Topics in Biophysics. Supplement
• Rocznik: 2016
• Tom: 39
• Numer: A: Plenary lectures
• Opis fizyczny: p.18,ref.

Twórcy

autor

Lazicka M.

• Department of Metabolic Regulation, Faculty of Biology, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland

autor

Grzyb J.

• Institute of Physics PAS, Al. Lotnikow 32/46, 02-668 Warsaw, Poland

Bibliografia

• [1] Grzyb J., Xu F., Nanda V., Łuczkowska R., Reijersee E., Lubitz W., Noy D. 2012. Empirical and computational design of iron-sulfur cluster proteins. BBA 1817, 1256-1262.
• [2] Grzyb J., Xu F., Weiner L., Reijerse E. J., Lubitz W., Nanda V., Noy D. 2010. De novo design of a non-natural fold for an iron–sulfur protein: Alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core. BBA 1797, 3, 406–413.
• [3] Zhang L., Ross Anderson J.L., Ahmed I., Norman J.A., Negron Ch., Mutter A.C., Dutton P.L., Koder R. 2011. Manipulating Cofactor Binding Thermodynamics in an Artificial Oxygen Transport Protein. Biochemistry, 50, 10254–10261.
• [4] Trammell S.A., Wang L., Zullo J.M., Shashidhar R., Lebedev N. 2004. Orientated binding of photosynthetic reaction centers on gold using Ni–NTA self-assembled monolayers. Biosens. Bioelectron. 19, 1649–1655.

Identyfikatory

DOI

10.1515/ctb-20163-0002