(Kis Petik Katalin)
Grammar/High School :
1984-88 1st place at Czechoslovak National Physics Olympiad ,1988
member of the Czechoslovak team on the International Physics Olympiad in 1987 and 1988.
1988-93 M.Sc.in physics, 1993
Faculty of Mathematics and Physics of Charles University in Prague.
Specialized in the physics of molecular and biological systems
Diploma thesis: "High temperature hole burning spectroscopy of porphyrin systems"
1993-99 Ph.D. in biology, 1999
"Structural biochemistry" program at the Eotvos Lorand University in Budapest, Hungary.
Thesis: "Identification of Protochlorophyllide structural forms in plants by fluorescence spectroscopy"
1999-2002 University of Illinois at Urbana-Champaign,
Laboratory for Fluorescence Dynamics.
Biophysics practice course for Hungarian and foreign students, (1st year of medicine, Semmelweis University) 1998/99, 2001/2002, 2002/2003
Hungarian Biophysics Society from 1995
Bolyai College 1995-1998
American Biophysical Society from 2000
English - good, Hungarian - native language, Czech - good, Slovak - good, Russian - basic level.
ABSTRACT OF THE PHD THESIS:
Identification of Protochlorophyllide structural forms in plants by fluorescence spectroscopy
Low temperature conventional and high resolution fluorescence spectroscopic
methods were applied to investigate the effect of the protein environment
on the structure and electronic energies of Mg- porphyrin derivatives in
native systems. The method was tested on a model system, Mg-mesoporphyrin
horseradish peroxidase (MgMP-HRP) and on its complex with a substrate,
naphtohydroxamic acid (NHA). As native systems of Mg- porphyrin derivatives
the protochlorophyllide (Pchlide) forms in the epicotyls of dark-grown
pea seedlings and wheat leaves have been studied.
The splitting of the lowest energy excited state of MgMP in HRP was characterized, and two structural forms of MgMP were identified. It was shown, that the binding of NHA reduces the structural variety in the configuration of MgMP to a single form with a more distorted structure and thus results in an enlarged splitting.
In the spectra of pea epicotyls, the fluorescence bands at 628 and 634-636~nm were studied. Based on the high resolution of the technique, the excitonic nature of these bands could be excluded, and the pure electronic (0,0) emission range of two monomeric forms of Pchlide was determined. The spectral difference was interpreted as a consequence of environmental effects of the surrounding matrix. On the basis of earlier results, the 636~nm form is considered as an enzyme-bound Pchlide and the 628~nm form as a Pchlide pool.
In dark-grown wheat leaves, three major spectral bands, with emission maxima at 633, 657 (of highest intensity) and 670~nm as Bands~I, II, and III were analyzed. It was shown, that Band~I is the envelope of three (0,0) emission bands with maxima at 628, 632 and 642~nm. Laser excitation studies in the range of Band~II at 10 K revealed the presence of a spectrally close donor and acceptor band. The intensity in Band~III originates mostly from being the vibronic satellite of Band~II, but contains also a small (0,0) band with absorption maximum at 674~nm. Besides the Pchlides with absorption around 650~nm within Band~II, another significant population of Band~I with absorption around 640~nm is also coupled by energy transfer to the acceptor of Band~II. The spectral difference between the two donor forms indicate different dipolar environments. Upon
increasing the temperature, the intensity of Band~II and of its satellite, Band~III decrease, while Band~I remains unaffected. Band~II shows also a broadening towards the blue side at higher temperatures. Both the quenching of fluorescence and the spectral change was explained by a thermally activated formation of a non-fluorescent intermediate state in the excited state of Pchlide acceptors.
CURRENT RESEARCH INTERESTS:
The amyloid-like structure of heat denatured human serum albumin
This project is related to the studies of Dr
Rita Galántai on the cofactor activity of denatured proteins
in plasmin activation process. To answer this question, we are investigating
the structural changes of human serum albumin (HSA) caused by heat denaturation
at different conditions. We are using fluorescent dyes that are routinely
used as indicators of amyloid structures.
1. E. Balog, K. Kis-Petik, J. Fidy, M. Koehler, J. Friedrich Interpretation
of multiple Q(0,0) bands in the absorption spectrum
of Mg-mesoporphyrin embedded in Horseradish Peroxidase, Biophys. J, 73 (1997) 397-405.
2. Levente Herenyi, Artur Suisalu, Katalin Kis-Petik, Koit Mauring,
Judit Fidy, Jaak Kikas. Variety in the coupling of a
prosthetic group to the apoprotein studied by energy selected fluorescence excitation and vibronic hole burning spectroscopy J.
Phys. Chem. B 102 (1998) 5932-5940.
3. B.Boddi, K. Kis-Petik, A.D. Kaposi, J. Fidy, C. Sundqvist. The two
spectroscopically different short wavelength
protochlorophyllide forms in pea epicotyl are both monomeric Biochim. Biophys. Acta, 1365 (1998) 531-540.
4. K. Kis-Petik, B. Boddi, A. D. Kaposi, J. Fidy. Identification of
protochlorophyllide forms in dark-grown wheat leaves by
conventional and laser excited fluorescence spectroscopy between 10 K-100 K, Photosynthesis Research, 60 (1999) 87-98
Kis-Petikova, K., Y. Chen, J. D. Müeller, and E. Gratton. Application of scanning fluorescence correlation spectroscopy for determination of particle shape. Biophys J., 78(1), 2603
Katarina Kis Petikova, Enrico Gratton
A method for distance measurement between fluorescent particles in the 10-200 nm range. Biophys J., 80(1),656.14