Wybrane publikacje

Drzewiecka-Matuszek A., Skalna A., Karocki A., Stochel G. and Fiedor L. (2005): Effects of heavy central metal on the ground and excited states of chlorophyll, J. Biol. Inorg. Chem. 10, 453-462;
Fiedor, L., Heriyanto, Fiedor, J., and Pilch, M. (2016): Effects of molecular symmetry on the electronic transitions in carotenoids, J. Phys. Chem. Lett. 7, 1821-1829;
Fiedor L., Kania A., Myśliwa-Kurdziel B., Orzeł Ł. and Stochel G. (2008): Understanding chlorophylls: central magnesium and phytyl as structural determinants, Biochim. Biophys. Acta 1777, 1491-1500;
Kania A. and Fiedor L. (2006): Steric control of bacteriochlorophyll ligation, J. Am. Chem. Soc. 128, 454-458;
Nowicka B., Kruk J. (2010): Occurrence, biosynthesis and function of isoprenoid quinones. BBA – Bioenergetics 1797, 1587-1605;
Szymańska R., Nowicka B., Kruk J. (2014): Hydroxy-plastochromanol and plastoquinone-C as singlet oxygen products during photooxidative stress in Arabidopsis. Plant Cell Environ. 37, 1464-1473;
Szymańska R., Kruk J. (2010): Plastoquinol is the Main Prenyllipid Synthesized During Acclimation to High Light Conditions in Arabidopsis and is Converted to Plastochromanol by Tocopherol Cyclase. Plant Cell Physiol. 51, 537-545.
J. Korohoda, K. Strzałka (1979): High efficiency genetic transformation in maize induced by exogenous DNA. Z. Pflanzenphysiol. 94, 95-99;
K. Strzałka, T. Sarna, J. S. Hyde (1986): ESR oxymetry: measurement of photosynthetic oxygen evolution by spin-probe technique. Photobiochem. Photobiophys. 12, 67-71;
K. Strzałka, J. Ngernprasirtsiri, A. Watanabe, T. Akazawa (1987): Sycamore amyloplasts can import and process precursors of nuclear encoded chloroplast proteins. Biochem. Biophys. Res. Commun. 149, 799-806;
K. Strzałka, T. Walczak, T. Sarna, H. M. Swartz (1990): Measurement of time-resolved oxygen concentration changes in photosynthetic systems by nitroxide-based EPR oximetry. Arch. Biochem. Biophys. 281, 321-318;
D. Latowski, H.-E. Akerlund, K. Strzałka (2004): Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. Biochemistry 43, 4417-4420;

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