Acta Biologica et Medica Germanica. / Band 38, Heft 2/3 / / hrsg. von R. Baumann.
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Table of Contents:
- Frontmatter
- INHALTSVERZEICHNIS
- SACHWORTVERZEICHNIS
- AUTORENVERZEICHNIS
- Preface
- A thermodynamic-kinetic analysis of the cytochrome P-450 heme pocket
- Cytochrome P-450Cam and putidaredoxin interaction during electron transfer
- Spin state transitions of liver microsomal cytochrome P-450
- Quantitative analysis of the spin equilibrium of cytochrome P-450 LM2 fraction from rabbit liver microsomes
- The importance of the spin equilibrium in cytochrome P-450 for the reduction rate of the heme iron
- Activated forms of oxygen in the metabolism of xenobiotics catalyzed by cytochrome P-450
- Comparison of spectral properties of 3-MC induced cytochrome P-448 from rabbits and rats
- Comparison of microsomal and solubilized monooxygenases from rat and rabbit by proton magnetic relaxation
- Stereochemical properties of the binding site of liver microsomal cytochrome P-450 as studied by substrate analogous spin labels
- Infrared spectral studies of carbon monoxide complexes of microsomal cytochromes P-450 and P-448
- Isolation, structural organization and mechanism of action of mitochondrial steroid hydroxylating systems
- Molecular properties of cytochrome P-45011/3 from adrenal cortex mitochondria
- Model systems for the coordination chemistry of cytochrome P-450
- The properties of cytochrome P-450 and hydroxylase activity of reconstituted pfoteoliposomal membranes
- Pituitary control of hepatic steroid metabolism
- Gas chromatography-mass spectrometry in analysis of protein amino acid composition
- Isolation and characterization of cytochrome P-450meg
- The alkane-hydroxylating enzyme system of the yeast Candida guilliermondii
- Mercaptide chelated protoheme : A model compound for cytochrome P-450
- The role of metal ions in oxygen activation
- Quantum chemical interpretation of the spectral properties of the GO and Oa complexes of hemoglobin and cytochrome P-450
- Catalytic properties of the liver microsomal hydroxylase system in reconstituted phospholipid vesicles
- Hydrodynamic studies on interactions between the components of the liver microsomal cytochrome P-450 system
- NADPH reduction of cytochrome P-450 at different integrational levels of the enzyme system
- Enzymatic activities of matrix-bound components of the liver microsomal cytochrome P-450 system
- Oxycytochrome P-450 : Its breakdown to superoxide for the formation of hydrogen peroxide
- NADPH-dependent electron transport chain in microsomes and lipid peroxidation catalyzed by metal ions
- Spectral properties of nonequilibrium states in cytochrome P-450 formed by reduction at subzero temperatures
- Mechanistic studies with purified components of the liver microsomal hydroxylation system: Spectral intermediates in reaction of cytochrome P-450 with peroxy compounds
- Kinetics of reduction of purified liver microsomal cytochrome P-450 in the reconstituted enzyme system studied by stopped flow spectrophotometry
- Electronic and steric factors in regioselective hydroxylation catalyzed by purified cytochrome P-450
- Interaction of cytochrome P-450 with hydrocarbons
- Comparison of the peroxidatic activity of cytochrome P-450 with other hemoproteins and model compounds
- Electrochemical investigations on the oxygen activation by cytochrome P-450
- The mechanism of hydroperoxide-dependent reactions with participation of cytochrome P-450
- CONTENTS
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