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PubMed1983

Kinetics of elementary steps in the cytochrome P-450 reaction sequence. VI. Model treatment of the NADPH-dependent first electron transfer reaction between cytochrome P-450 reductase and cytochrome P-450 LM2 in solution.

The NADPH-dependent reduction of P-450 LM2 has been studied both anaerobically and aerobically in solution state. The disintegration of the constitutive proteins was obtained by means of Triton N-101. At varied P-450 reductase/P-450 ratios two sets of reaction curves were treated by computer procedures. A general reaction mechanism of a modified Michaelis-Menten type could be evidenced. Rate determination in the overall reaction could be proved to be exerted by the electron transfer in the P-450 reductase/P-450 intermediate complex. This process is unresolved as yet. The significance of the solution state investigations is outlined with respect to the functional clusters in microsomes and liposomes, respectively. The physiologically relevant cluster reduction is supposed to follow similar kinetics based on a rapid protein exchange in the clusters.

Aerobiosis↗
PubMed1983

Spectrally distinct cytochrome b-563 components in a chloroplast cytochrome b-f complex: Interaction with a hydroxyquinoline N-oxide.

The two heme equivalents of cytochrome b-563 in the photosynthetic cytochrome b-f complex can be distinguished by their rate of reduction with dithionite at 25 degrees C and by their optical absorption spectra at 77 K. The cytochrome b component that is rapidly reduced after addition of dithionite or reduced ferredoxin possesses an alpha band that splits at 77 K into two peaks, at 557 and 561 nm. Prolonged incubation with reductant reveals a second, approximately equimolar cytochrome b component that has at 77 K an unsplit alpha-band maximum at 561 nm. The designations cytochrome b-563(H) and cytochrome b-563(L), respectively, are proposed for the rapidly and more slowly reduced cytochrome b-563 components. Potentiometric titration establishes a midpoint potential, E(m), of -30 mV (electron change n approximately 2) for cytochrome b-563(H) and -150 mV (n = 1) for cytochrome b-563(L) at pH 7.5. The reduction potential of these components is raised by 2-heptyl-4-hydroxyquinoline N-oxide, giving E(m) values of +57 and -34 mV, respectively, with each titration slope approximating n = 2.

Journal Article↗
PubMed2002

Natural resistance to inhibitors of the ubiquinol cytochrome c oxidoreductase of Rubrivivax gelatinosus: sequence and functional analysis of the cytochrome bc(1) complex.

Biochemical analyses of Rubrivivax gelatinosus membranes have revealed that the cytochrome bc(1) complex is highly resistant to classical inhibitors including myxothiazol, stigmatellin, and antimycin. This is the first report of a strain exhibiting resistance to inhibitors of both catalytic Q(0) and Q(i) sites. Because the resistance to cytochrome bc(1) inhibitors is primarily related to the cytochrome b primary structure, the petABC operon encoding the subunits of the cytochrome bc(1) complex of Rubrivivax gelatinosus was sequenced. In addition to homologies to the corresponding proteins from other organisms, the deduced amino acid sequence of the cytochrome b polypeptide shows (i) an E303V substitution in the highly conserved PEWY loop involved in quinol/stigmatellin binding, (ii) other substitutions that could be involved in resistance to cytochrome bc(1) inhibitors, and (iii) 14 residues instead of 13 between the histidines in helix IV that likely serve as the second axial ligand to the b(H) and b(L) hemes, respectively. These characteristics imply different functional properties of the cytochrome bc(1) complex of this bacterium. The consequences of these structural features for the resistance to inhibitors and for the properties of R. gelatinosus cytochrome bc(1) are discussed with reference to the structure and function of the cytochrome bc(1) complexes from other organisms.

Amino Acid Sequence↗
PubMed1977

The effect of banol and paraoxon on the NADPH-cytochrome c reductase activity and cytochrome P-450 content in rats.

We investigated the effect of banol and paraoxon on the activity of NADPH-cytochrome c reductase and cytochrome P-450 concentration in microsomes of rats treated in vivo with these compounds alone, or in the presence of phenobarbitone. The results showed that banol reduced the NADPH-cytochrome c reductase activity and the concentration of cytochrome P-450, while paraoxon reduced the activity of NADPH-cytochrome c reductase, but increased the cytochrome P-450 concentration. Phenobarbitone stimulated an increased NADPH-cytochrome c reductase activity and cytochrome P-450 concentration. When applied with banol and paraoxon, phenobarbitone lowered their inhibitory effect.

Animals↗
PubMed1984

Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase.

The interaction between cytochrome c and cytochrome c peroxidase was investigated using sedimentation equilibrium at pH 6,20 degrees C, in a number of buffer systems varying in ionic strength between 1 and 100 mM. Between 10 and 100 mM ionic strengths, the sedimentation of the individual proteins was essentially ideal, and sedimentation equilibrium experiments on mixtures of the two proteins were analyzed assuming ideal solution behavior. Analysis of the distribution of mixtures of cytochrome c and cytochrome c peroxidase in the ultracentrifuge cell based on a model involving the formation of a 1:1 cytochrome c-cytochrome c peroxidase complex gave values of the equilibrium dissociation constant ranging from 2.3 +/- 2.7 microM at 10 mM ionic strength to infinity (no detectable interaction) at 100 mM ionic strength. Attempts to determine the presence of complexes involving two cytochrome c molecules bound to cytochrome c peroxidase were inconclusive.

Cytochrome c Group↗
PubMed1991

Cytochrome P450 IIIA1 (P450p) requires cytochrome b5 and phospholipid with unsaturated fatty acids.

In contrast to other P450 enzymes purified from rat liver microsomes, purified P450 IIIA1 (P450p) is catalytically inactive when reconstituted with NADPH-cytochrome P450 reductase and the synthetic lipid, dilauroylphosphatidylcholine. However, purified P450 IIIA1 catalyzes the oxidation of testosterone when reconstituted with NADPH-cytochrome P450 reductase, cytochrome b5, an extract of microsomal lipid, and detergent (Emulgen 911). The present study demonstrates that the microsomal lipid extract can be replaced with one of several naturally occurring phospholipids, but not with cholesterol, sphingosine, sphingomyelin, ceramide, cerebroside, or cardiolipin. The ratio of the testosterone metabolites formed by purified P450 IIIA1 (i.e., 2 beta-, 6 beta-, and 15 beta-hydroxytestosterone) was influenced by the type of phospholipid added to the reconstitution system. The ability to replace microsomal lipid extract with several different phospholipids suggests that the nature of the polar group (i.e., choline, serine, ethanolamine, or inositol) is not critical for P450 IIIA1 activity, which implies that P450 IIIA1 activity is highly dependent on the fatty acid component of these lipids. To test this possibility, P450 IIIA1 was reconstituted with a series of synthetic phosphatidylcholines. Those phosphatidylcholines containing saturated fatty acids were unable to support testosterone oxidation by purified P450 IIIA1, regardless of the acyl chain length (C6 to C18). In contrast, several unsaturated phosphatidylcholines supported testosterone oxidation by purified P450 IIIA1, and in this regard dioleoylphosphatidylcholine (PC(18:1)2) was as effective as microsomal lipid extract and naturally occurring phosphatidylcholine or phosphatidylserine. These results confirmed that P450 IIIA1 activity is highly dependent on the fatty acid component of phospholipids. A second series of experiments was undertaken to determine whether microsomal P450 IIIA1, like the purified enzyme, is dependent on cytochrome b5. A polyclonal antibody against purified cytochrome b5 was raised in rabbits and was purified by affinity chromatography. Anti-cytochrome b5 caused a approximately 60% inhibition of testosterone 2 beta-, 6 beta-, and 15 beta-hydroxylation by purified P450 IIIA1 and inhibited these same reactions by approximately 70% when added to liver microsomes from dexamethasone-induced female rats. Overall, these results suggest that testosterone oxidation by microsomal cytochrome P450 IIIA1 requires cytochrome b5 and phospholipid containing unsaturated fatty acids.

Animals↗