C. Jung

发表

Epitope mapping of cytochrome P450cam (CYP101).

A. Archakov, G. H. Hoa, S. Kozin, 1997, Archives of biochemistry and biophysics.

Cytochrome P450 biosensors-a review.

Ulla Wollenberger, Frieder W Scheller, U. Wollenberger, 2005, Biosensors & bioelectronics.

Spectroscopic studies of peroxyacetic acid reaction intermediates of cytochrome P450cam and chloroperoxidase.

J. Terner, V. Schünemann, A. Trautwein, 2002, Journal of inorganic biochemistry.

Spectroelectrochemistry of Redox Enzymes

U. Wollenberger, F. Scheller, T. Ruzgas, 2006 .

Conformational transitions and redox potential shifts of cytochrome P450 induced by immobilization

P. Hildebrandt, S. Todorović, D. Murgida, 2005, JBIC Journal of Biological Inorganic Chemistry.

A new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain.

J. Peterson, C. Jung, A. Kariakin, 2002, Biochemistry.

The Glo3 GAP crystal structure supports the molecular niche model for ArfGAPs in COPI coats.

C. Jung, A. Kendall, L. Jackson, 2021, Advances in biological regulation.

Intermediates in the reaction of substrate‐free cytochrome P450cam with peroxy acetic acid

V. Schünemann, A. Trautwein, R. Weiss, 2000, FEBS letters.

The proton activity at cryogenic temperatures--a possible influence on the spin state of the heme iron of cytochrome P-450cam in supercooled buffered solutions.

O. Ristau, H. Schulze, C. Jung, 1994, Biochimica et biophysica acta.

Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration.

R. Bernhardt, R. Schwarzer, C. Jung, 2000, Biochemical and biophysical research communications.

Tyrosine Radical Formation in the Reaction of Wild Type and Mutant Cytochrome P450cam with Peroxy Acids

S. Sligar, A. Barra, V. Schünemann, 2004, Journal of Biological Chemistry.

Changes in secondary structure and salt links of cytochrome P-450cam induced by photoreduction: a Fourier transform infrared spectroscopic study.

C. Jung, J. Contzen, 1999, Biochemistry.

Role of the polarity of the heme environment for the CO stretch modes in cytochrome P-450cam-CO.

E. Deprez, H. Schulze, C. Jung, 1996, Biochemistry.

An INDO-CI method in π-approximation for the calculation of transition metal complexes with organic ligands—application to iron(II)-trisdiimine complexes

O. Ristau, C. Jung, C. Jung, 1983 .

Electrochemically driven biocatalysis of the oxygenase domain of neuronal nitric oxide synthase in indium tin oxide nanoparticles/polyvinyl alcohol nanocomposite.

U. Wollenberger, Songqin Liu, J. Qian, 2013, Bioelectrochemistry.

The CO stretching mode infrared spectrum of substrate-free cytochrome P-450cam-CO: the effect of solvent conditions, temperature, and pressure.

S. Sligar, O. Ristau, H. Schulze, 1996, European journal of biochemistry.

Quantum chemical calculations of porphyrin systems. The spectral differences between the dication and the dianion

C. Jung, 1979 .

Generation of carbon monoxide and iron from hemeproteins in the presence of 7,8-dihydroneopterin.

G. Reibnegger, R. Möller, E. Tafeit, 2002, Biochimica et biophysica acta.

Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450

A. Barra, V. Schünemann, A. Trautwein, 2005, Biological chemistry.

Brown's bond valences, a measure of the strength of hydrogen bonds

J. Lösel, H. Lutz, C. Jung, 1995 .

Quantum chemical explanation of the “hyper” spectrum of the carbon monoxide complex of cytochrome P-450

C. Jung, 1985 .

Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs)

C. Jung, 2008, Analytical and bioanalytical chemistry.

The mystery of cytochrome P450 Compound I: a mini-review dedicated to Klaus Ruckpaul.

C. Jung, 2011, Biochimica et biophysica acta.

Substrate binding favors enhanced NO binding to P450cam.

R. van Eldik, G. Stochel, Alicja Franke, 2004, Journal of the American Chemical Society.

Hydrogen bonding in solid hydroxides with strongly polarising metal ions, β-Be(OH)2 and ε-Zn(OH)2

H. Lutz, C. Jung, H. Jacobs, 1998 .

Water molecules and hydroxide ions in condensed materials; correlation of spectroscopic and structural data☆

H. Lutz, C. Jung, 1997 .

Use of vibrational spectroscopy to study protein and DNA structure, hydration, and binding of biomolecules: A combined theoretical and experimental approach

K. Frimand, R. Wade, S. Suhai, 2006 .

Crystal Structures and Hydrogen Bonding for β-Be(OH)2 and ε-Zn(OH)2.

W. Kockelmann, H. Lutz, C. Jung, 1998 .

FT-Infrared spectroscopic studies of the iron ligand CO stretch mode of iNOS oxygenase domain: effect of arginine and tetrahydrobiopterin.

D. Stuehr, C. Jung, D. Ghosh, 2000, Biochemistry.

Leakage in cytochrome P450 reactions in relation to protein structural properties

C. Jung, 2007 .

Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy

C. Jung, 2000, Journal of molecular recognition : JMR.

Low-temperature FTIR spectra and hydrogen bonds in polycrystalline adenosine and uridine.

G. Shoham, C. Jung, M. Rozenberg, 2005, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

Ordered and disordered hydrogen bonds in adenosine, cytidine and uridine studied by low temperature FT infrared spectroscopy

G. Shoham, C. Jung, M. Rozenberg, 2003 .

Low temperature FTIR spectra and hydrogen bonds in polycrystalline cytidine.

G. Shoham, C. Jung, M. Rozenberg, 2004, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

Step-scan time-resolved FTIR spectroscopy of cytochrome P-450cam carbon monoxide complex: a salt link involved in the ligand-rebinding process.

C. Jung, J. Contzen, 1998, Biochemistry.

Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.

G. Snatzke, C. Jung, B. Nölting, 1992, Biochimica et biophysica acta.

FTIR studies of the redox partner interaction in cytochrome P450: the Pdx-P450cam couple.

R. Wade, Domantas Motiejūnas, C. Jung, 2007, Biochimica et biophysica acta.

Thermostability and Ca2+ binding properties of wild type and heterologously expressed PsbO protein from cyanobacterial photosystem II.

W. Saenger, B. Loll, K. Irrgang, 2005, Biochemistry.

Antigenic mapping of bacterial and animal cytochromes P-450.

A. Archakov, S. Kozin, G. Hui Bon Hoa, 1996, Biochimie.

Mobility of norbornane-type substrates and water accessibility in cytochrome P-450cam.

G. H. Hoa, H. Schulze, C. Jung, 1997, Biochimica et biophysica acta.

Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3.

P. Souček, N. Bec, A. Munro, 2000, European journal of biochemistry.

Spectroscopic characterization of cytochrome P450 Compound I.

S. de Vries, V. Schünemann, C. Jung, 2011, Archives of biochemistry and biophysics.

Freeze-quenched iron-oxo intermediates in cytochromes P450.

V. Schünemann, C. Jung, F. Lendzian, 2005, Biochemical and biophysical research communications.

Proton nuclear magnetic resonance study of the binary complex of cytochrome P450cam and putidaredoxin: interaction and electron transfer rate analysis

Richard G. S. Spencer, A. Bondon, G. Hui Bon Hoa, 1999, FEBS letters.

The carbon monoxide stretching modes in camphor-bound cytochrome P-450cam. The effect of solvent conditions, temperature, and pressure.

O. Ristau, H. Schulze, C. Jung, 1994, European journal of biochemistry.

Clay-bridged electron transfer between cytochrome p450(cam) and electrode.

F W Scheller, U Wollenberger, U. Wollenberger, 2000, Biochemical and biophysical research communications.

Compressibility and uncoupling of cytochrome P450cam: high pressure FTIR and activity studies.

G. H. Hoa, S. Kozin, J. Chervin, 2003, Biochemical and biophysical research communications.

Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101). A high-pressure stopped-flow study.

N. Bec, R. Lange, C. Jung, 2002, European journal of biochemistry.

Substrate analogue induced changes of the CO-stretching mode in the cytochrome P450cam-carbon monoxide complex.

J. Doucet, G. H. Hoa, C. Jung, 1992, Biochemistry.

Autocatalytic nitration of P450CAM by peroxynitrite.

A. Daiber, C. Schöneich, V. Ullrich, 2000, Journal of inorganic biochemistry.

Apocytochrome P450cam is a native protein with some intermediate-like properties.

W. Pfeil, C. Jung, B. Nölting, 1993, Biochemistry.

Intermolecular electron transfer in cytochrome P450cam covalently bound with Tris(2,2'-bipyridyl)ruthenium(II): structural changes detected by FTIR spectroscopy.

R. Kraft, S. Kostka, C. Jung, 2002, Journal of inorganic biochemistry.

Time‐resolved Fourier‐transform infrared studies of the cytochrome P‐450cam carbonmonoxide complex bound with (1R)‐camphor and (1S)‐camphor substrate

O. Ristau, C. Jung, J. Contzen, 1996, FEBS letters.

Substrate induced changes of the active site electronic states in reduced cytochrome P450 cam and the photolysis product of its CO complex

C. Jung, S. Greschner, Y. Sharonov, 1993, FEBS letters.

Quantum-chemical interpretation of the unusual absorption spectrum of the cytochrome P-450CO complex

O. Ristau, C. Jung, 1977 .

Multi‐frequency EPR and Mössbauer spectroscopic studies on freeze‐quenched reaction intermediates of nitric oxide synthase

A. Barra, V. Schünemann, A. Trautwein, 2005, Magnetic resonance in chemistry : MRC.

Mössbauer- and EPR-Snapshots of an Enzymatic Reaction: The Cytochrome P450 Reaction Cycle

A. Barra, V. Schünemann, A. Trautwein, 2004 .

Mössbauer and EPR Study of Reaction Intermediates of Cytochrome P450

J. Terner, V. Schünemann, A. Trautwein, 2002 .

Cytochrome P-450-CO and substrates: lessons from ligand binding under high pressure.

C. Jung, 2002, Biochimica et biophysica acta.

Study of H2O2-supported N-demethylations catalyzed by cytochrome P-450 and horseradish peroxidase.

W. Damerau, F. Scheller, R. Renneberg, 1983, Biochemical and biophysical research communications.

Binding sites of pyridine in cytochrome P-450cam.

O. Ristau, C. Jung, 1991, Biochimica et biophysica acta.

Metal-metal interactions involving metalloporphyrins. II. The inner-sphere reduction of tetraphenylporphineiron (3) chloride by chromium (II) in benzene.

C. Jung, I. Cohen, T. Governo, 1972, Journal of the American Chemical Society.

Crystal structure of cytochrome P‐450cam complexed with the (1S)‐camphor enantiomer

I. Schlichting, I Schlichting, C Jung, 1997, FEBS letters.

Multiple molecular recognition mechanisms. Cytochrome P450--a case study.

Rebecca C Wade, Sudarko, R. Wade, 2005, Biochimica et biophysica acta.

High Pressure as Tool to Study Structural Properties of Thiolate Heme Proteins

J. Chervin, B. Canny, C. Jung, 2003 .

Comparative Fourier transform infrared studies of the secondary structure and the CO heme ligand environment in cytochrome P-450cam and cytochrome P-420cam.

A. Bondon, C. Jung, G. Simonneaux, 1997, Biochemistry.

Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor.

R. Wade, G. H. Hoa, V. Helms, 1996, Biochemistry.

Compressibility of the heme pocket of substrate analogue complexes of cytochrome P-450cam-CO. The effect of hydrostatic pressure on the Soret band.

K. Heremans, E. Gill, G. Hui Bon Hoa, 1995, European journal of biochemistry.

Substrate interactions in cytochrome P‐450: correlation between carbon‐13 nuclear magnetic resonance chemical shifts and C‐O vibrational frequencies

A. Bondon, E. Gill, C. Jung, 1995, FEBS letters.

Quantum chemical interpretation of the spectral properties of the CO and O2 complexes of hemoglobin and cytochrome P-450.

O. Ristau, J. Friedrich, C. Jung, 1979, Acta biologica et medica Germanica.

Structural stability and dynamics of hydrogenated and perdeuterated cytochrome P450cam (CYP101).

D. Myles, F. Meilleur, C. Jung, 2004, Biochemistry.

About Oxygen, Cytochrome P450 and Titanium: Learning from Ron Estabrook

C. Jung, 2007, Drug metabolism reviews.

Thermodynamic properties of apocytochrome P450cam

W. Pfeil, C. Jung, B. Nölting, 1993 .