• Publications
  • Influence
Rotational diffusion of cytochrome P-450 in the microsomal membrane-evidence for a clusterlike organization from saturation transfer electron paramagnetic resonance spectroscopy.
Rotational diffusion of cytochrome P-450 in rabbit liver microsomes has been studied by saturation transfer EPR spectroscopy. Sulfhydryl groups of cytochrome P-450 were selectively modified using aExpand
  • 40
  • 1
Membrane topology of microsomal cytochrome P-450: saturation transfer EPR and freeze-fracture electron microscopy studies.
The rotation of cytochrome P-450 LM2 (CYPIIB4) incorporated into large microsomal-like lipid vesicles was investigated by saturation transfer EPR using 15N- and 2H-substituted spin labels. InExpand
  • 37
  • 1
NADPH and H2O2‐dependent reactions of cytochrome P‐450LM compared with peroxidase catalysis
Cytochrome P-450 has been shown not only to act as monooxygenase by activating molecular oxygen but also to catalyze substrate hydroxylation supported by various organic hydroperoxides as well as byExpand
  • 35
  • 1
Mobility and clusterlike organization of liposomal cytochrome P-450 LM2: saturation transfer EPR studies.
Rotational diffusion of the electrophoretically homogenenous isozyme cytochrome P-450 LM2 from rabbit liver microsomes has been studied in buffer solution and in phospholipid vesicles by means ofExpand
  • 7
Selective removal of spectral components in complex ST-EPR spectra of spin-labeled cytochrome P-450
Abstract Incubation of cytochrome P-450 spin labeled by an isocyanide derivative with K 3 Fe(CN) 6 results in a selective disappearance of the spectral components attributable to the weaklyExpand
  • 8
Binding behaviour of substrate analogous spin‐labelled n‐alkylamines in liver microsomal cytochrome P‐450
The binding affinity of alkylamines (type II substrates) to cytochrome P-450 from liver microsomes increases with elongation of the alkyl side chain [l] . These investigations revealed thatExpand
  • 11
  • PDF
Motional dynamics of a spin labeled substrate analogue bound to cytochrome P-450: saturation transfer EPR studies.
The rotational motion of the spin labeled substrate analogue n- propylisocyanide bound to the active center of cytochrome P-450 was studied by saturation transfer EPR. The observed motional rateExpand
  • 3
Studies on the active center of cytochrome P-450 using a spin-labeled type I substrate analogue
Abstract The binding of an active-site-targeted spin-labeled compound to cytochrome P -450 showing type I spectral characteristics in its optical difference spectrum was studied by optical and EPRExpand
  • 3
Spin‐labelled isocyanides as stereochemical probes for the active center of cytochrome P‐450
Spin-labelled substrate analogues have been widely used to obtain a deeper insight into stereochemical properties of the active sites of enzymes [ 1,2]. In this way the spin-labelled inhibitorExpand
  • 10
Hydrazinverbindungen als Heterobestandteile in Peptiden. XIII. Nα‐Acylierung von Hydrazinoessigsäure‐Derivaten und Synthese von Eledoisin‐Octapeptiden mit Nα‐acetylierter Hydrazinoessigsäure anstelle
Die Nα-Acylierung von Nβ-Acylhydrazinoessigsaure-Derivaten wird mit Saurechloriden in Pyridin durchgefuhrt. Mit Hilfe von N-Methylacetamidchlorid in situ erhaltene Chloride von Z-Aminosauren werdenExpand
  • 6