Katarína Kis-Petiková PhD (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.

University:
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"

Ph.D. studies:
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"

Post-doctoral work:
1999-2002   University of Illinois at Urbana-Champaign,
                    Laboratory for Fluorescence Dynamics.

PROFESSIONAL EXPERIENCES:
 

•      Research group of  Dr. Jan Hala in low temperature laser laboratory at the Department of Chemical Physics, Prague.  1991-1993 (hole burning spectroscopy, fluorescence spectroscopy of porphyrin solutions)
•      Research group of Gyorgy Varo at the Institute of Biophysics, Research institute Szeged 1991, one month (measurements on bacteriorhodopsin)
•      Research group of  Dr. Janos Hunyadi at the Department of Dermatology, Medical University of Debrecen. 1993-1994, ten months (immunological measurements, work with cell cultures)
•      Research group of  Dr. Judit Fidy at a luminescence spectroscopy laboratory of the Institute of Biophysics at the Semmelweis University of Medicine. 1994-1998 (fluorescence line narrowing, conventional fluorescence spectroscopy   of porphyrins embedded in protein and native systems, sample preparation)
•      Physics of biological systems: From molecules to species, European- Nordic Summer School and Workshop, Humlebaek, Denmark, 1995. two weeks
•      Research group of  Dr. Jaak Kikas, Institute of Physics, Estonian Academy of Sciences, Tartu, Estonia 1998, two weeks (fluorescence line narrowing, hole burning spectroscopy of etiolated leaves)
•      Research group of  Dr. Enrico Gratton,  Laboratory for Fluorescence Dynamics, University of Illinois at Urbana-Champaign, from 1999 until 2002, two years. (fluorescence correlation spectroscopy, distance measurement with  circular scanning-development of a new methodology)

TEACHING EXPERIENCE:

     Biophysics practice course for Hungarian and  foreign students, (1st year of medicine, Semmelweis University) 1998/99, 2001/2002, 2002/2003

MEMBERSHIP:

     Hungarian Biophysics Society from 1995
     Bolyai College 1995-1998
     American Biophysical Society from 2000

LANGUAGE SKILLS:

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.
 

PUBLICATIONS:

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

Abstracts:

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