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PubMed1977

Cytochrome b5 and cytochrome b5 reductase-phospholipid vesicles. Intervesicle protein transfer and oreintation factors in protein-protein interactions.

NADH-cytochrome b5 reductase readily binds to preformed phospholipid vesicles either below or above the phase transition temperature of the lipid and in the absence of detergents. The isolated vesicles are free of unbound reductase, and the lipid is present as small, closed bilayers (250 to 400 A in diameter) as indicated by gel filtration, density gradient centrifugation, and internal volume measurements with [3H]glucose. The order of substrate specificity of the bound reductase is: ferricyanide = cytochrome b5 bound to reductase vesicles (100%) greater than cytochrome b5 heme peptide (13%) greater than unbound cytochrome b5 (4.5%) greater than cytochrome b5 vesicles (0.1%). This indicates that a specific orientation of cytochrome b5 and reductase in the bilayer is required for optimal interaction. Protein transfer occurs between reductase vesicles and cytochrome b5 vesicles. The transfer is time-dependent (40 to 70% complete in 2 h), does not involve vesicle fusion, is most rapid at the phase transition temperature of the phospholipid, and appears to require a fluid bilayer.

Animals↗
PubMed1996

Genetic analysis of factors controlling high-level expression of cytochrome P450, CYP6D1, cytochrome b5, P450 reductase, and monooxygenase activities in LPR house flies, Musca domestica.

To understand better the biochemical genetics of cytochrome P450 monooxygenase-mediated insecticide resistance, we examined the microsomal monooxygenases in insecticide-susceptible (aabys) and pyrethroid-resistant (LPR) house fly strains, as well as 15 house fly lines derived from crosses of LPR and aabys. In comparison to the aabys strain, LPR had higher levels of total cytochromes P450, cytochrome b5, P450 reductase, CYP6D1, and three P450 monooxygenase activities: 7-ethoxycoumarin O-deethylase (ECOD), methoxyresorufin O-demethylase (MROD), and aromatic hydrocarbon hydroxylase (AHH). The elevated levels of cytochrome b5 were linked to factors on autosomes 1 and 2. This is similar to previous reports on monooxygenase-mediated resistance and is consistent with the idea that elevated cytochrome b5 levels are involved in monooxygenase-mediated resistance in the LPR strain. Linkage of the elevated P450 reductase is different from that of monooxygenase-mediated resistance. Strains having high levels of CYP6D1 (i.e., like LPR) had high levels of P450 reductase, while strains having intermediate levels of CYP6D1 also had high levels of reductase. Therefore, there is no clear evidence that the elevated P450 reductase in the LPR strain is required for the increased monooxygenase activity. Overexpression of total cytochromes P450, CYP6D1 (mRNA and protein), and CYP6D1-mediated monooxygenase activities (MROD and AHH) in LPR microsomes was linked to a combination of factors on autosomes 1 and 2. This demonstrates that increased expression of CYP6D1 in the LPR strain is both cis regulated by a factor(s) on autosome 1 and trans regulated by a factor(s) on autosome 2. The correlation between the overexpression of CYP6D1 mRNA and protein suggests that CYP6D1 expression is regulated transcriptionally. Monooxygenase-mediated resistance in LPR is controlled by factors on autosomes 1 and 2, which supports previous claims that CYP6D1 is responsible for monooxygenase-mediated resistance in the LPR strain.

Animals↗
PubMed2003

QcrCAB operon of a nocardia-form actinomycete Rhodococcus rhodochrous encodes cytochrome reductase complex with diheme cytochrome cc subunit.

Structural genes encoding quinol-cytochrome c reductase (QcR) were cloned and sequenced from nocardia-form actinomycete Rhodococcus rhodochrous. QcrC and qcrA encode diheme cytochrome cc and the Rieske Fe-S protein, respectively, while the qcrB product is a diheme cytochrome b. These amino acid sequences are similar to those of Corynebacterium and Mycobacterium, the members of high G+C content firmicutes. The presence of diheme cytochrome cc subunit as a sole c-type cytochrome in these organisms suggests the direct elecron transfer to cytochrome c oxidase. The N-terminal half of the Rieske Fe-S proteins of these bacteria has a unique structure with three transmembrane helices, while the C-terminal half sequence is conserved. A phylogenetic tree using the latter region showed that high G+C firmicutes form a clear clade with Thermus, but not with low G+C firmicutes.

Amino Acid Sequence↗
PubMed1988

Redox cycling of bleomycin-Fe(III) and DNA degradation by isolated NADH-cytochrome b5 reductase: involvement of cytochrome b5.

Isolated and purified microsomal NADH-cytochrome b5 reductase (EC 1.6.2.2) was incubated with bleomycin (BLM) and FeCl3 in the presence of NADH. Only when purified cytochrome b5 was added could an increased NADH consumption be observed indicating redox cycling of the BLM-Fe(III) complex. In the presence of DNA, BLM-Fe(III)-related NADH consumption was accompanied by malondialdehyde (MDA) formation, further evidence for BLM activation yielding oxidative DNA cleavage. BLM, FeCl3, cytochrome b5 and NADH were absolutely necessary to provide these effects. Addition of DNA changed the initial velocity (V0) and the shape of the NADH consumption curves, both probably due to an interaction between DNA and BLM-Fe(III). Furthermore, DNA effectively protected BLM-Fe(III) from autoxidative degradation during redox cycling. BLM-Fe(III)-related, reductase-catalyzed NADH consumption and MDA formation were also dependent on oxygen, showing the involvement of oxygen in the reduction process and in the action of the drug-metal complex in attacking DNA. However, superoxide dismutase (EC 1.15.1.1) and catalase (EC 1.11.1.6) did not affect NADH consumption. Also, superoxide dismutase and catalase were almost without influence on MDA formation, suggesting that no free (or freely accessible) reactive oxygen species occurred during the redox cycle and DNA damage. The results reveal that the BLM-Fe(III) complex undergoes redox cycling by the microsomal NADH-dependent cytochrome b5 reductase-cytochrome b5 system. The significance of this effect for the action of BLM and the involvement of cytochrome b5 is discussed with regard to the presence of these enzymes in the cell nucleus.

Animals↗
PubMed1981

Neonatal imprinting and hepatic cytochrome P-450. II. Partial purification of a sex-dependent and neonatally imprinted form(s) of cytochrome P-450.

A new form of cytochrome P-450 was partially purified from hepatic microsomes of neonatally imprinted rats (adult male and adult male castrated at four weeks of age). This new form of cytochrome P-450 appears to have an apparent molecular weight of approximately 50,000 daltons as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It appears that this form of cytochrome P-450 is either absent or present in low concentrations in cytochrome P-450 preparations isolated from neonatally nonimprinted rats (adult female and adult male castrated at birth). Reconstitution of testosterone hydroxylase and benzphetamine N-demethylase activities of this partially purified cytochrome P-450 revealed that the presence of testosterone 16 alpha-hydroxylase activity, an imprintable microsomal enzyme, was in parallel with the imprinting status of the animals; a significantly higher activity was detected in the neonatally imprinted than that of the nonimprinted animals. This was in contrast to the nonimprintable benzphetamine N-demethylase, testosterone 7 alpha- and 6 beta-hydroxylase activities which exhibited no correlation with the imprinting status of the animals. We have prepared antisera from rabbits using the partially purified cytochrome P-450 preparations from adult male rats as antigens. These antisera inhibited microsomal testosterone 16 alpha- and 7 alpha-hydroxylase activities in a concentration-dependent manner, without impairing 6 beta-hydroxylase activity. These data suggest that the partially purified cytochrome P-450 from adult male rats consists of both imprintable (16 alpha-) and nonimprintable (7 alpha-) testosterone hydroxylase activities.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Mutations in the structural gene for cytochrome c result in deficiency of both cytochromes aa3 and c in Neurospora crassa.

The cyt-12-12 mutant of Neurospora crassa is characterized by slow growth and a deficiency of spectrophotometrically-detectable cytochromes aa3 and c. Using a sib-selection procedure we have isolated the cyt-12+ allele from a cosmid library of N. crassa genomic DNA. Characterization of the cyt-12+ allele reveals that it encodes the structural gene for cytochrome c. DNA sequence analysis of the cyt-12-12 allele revealed a mutation in the cytochrome c coding sequence that results in replacement of a glycine residue, which is invariant in the cytochrome c of other species, with an aspartic acid. Genetic analysis confirms that cyt-12-12 is allelic with the previously-characterized cyc-1-1 mutant, which was also shown to affect the single locus encoding cytochrome c in N. crassa. We suggest that the amount of functional cytochrome c present in mitochondria influences the level of cytochrome aa3.

Alleles↗
PubMed1977

Structure of cytochrome c oxidase from baker's yeast - a progress report. Preparation of four subunits for amino acid sequence determination and attempts to localize the cytochrome c binding site.

Cytochrome c oxidase from the inner membrane of yeast mitochondria consists of seven nonidentical protein subunits, three being synthesized on mitochondrial ribosomes (molecular weights I: 43 K, II: 34 K, and III: 24 K) and four being made on cytoplasmic ribosomes (molecular weights IV: 14 K, V: 12 K, VI: 12 K, and VII: 4.5 K). In the present study all four cytoplasmically synthesized subunits of the enzyme were isolated on a large scale using ion exchange chromatography and gel filtration. Their amino acid composition as well as their amino- and carbosy-terminal amino acid residues have been determined. Sequence determinations of subunits IV and VI are already in an advanced state. The sequence of subunit VI is characterized by a large amino-terminal stretch dominated by charged amino acid residues followed by a cluster of hydrophobic amino acids. The binding site of yeast cytochrome oxidase for cytochrome c was studied by chemical crosslinking experiments. The formation of a disulfide bridge between the two proteins was observed by using cytochrome c from yeast modified with 5-thionitrobenzoate at the cysteinyl residue in position 107. Alternatively, a disulfide between yeast cytochrome c and the oxidase could be formed directly by oxidation with copper phenanthroline. Gel electrophoresis of the crosslinked complexes in sodium dodecyl sulfate revealed a new protein band with an apparent molecular weight of 38 K. This new band appears to be derived from cytochrome c and from subunit III of cytochrome oxidase.

Amino Acid Sequence↗
PubMed1995

Effect of hypothyroidism on the expression of cytochrome c and cytochrome c oxidase in heart and muscle during development.

The effect of thyroid hormone on the expression of mitochondrial proteins was evaluated during development by measuring cytochrome c oxidase (CYTOX) activity and cytochrome c protein and mRNA levels in heart and skeletal muscle of control and hypothyroid rats. Animals were killed at the late fetal, early, and late postnatal stages up to 56 days of age. In heart, CYTOX activity increased 2.3-fold above the fetal level throughout development, most of which occurred prior to 2 days of age. No increase was observed in muscle. CYTOX activity was reduced in hypothyroid animals throughout development in heart compared to controls (by 50% at 56 days), but in muscle no effect of hypothyroidism was observed. In muscle and heart 4- and 1.5-fold increases in cytochrome c above the fetal level were evident by 1 day of age, with further increases to 8.5- and 2.7-fold by 56 days, respectively. The increase in cytochrome c differed from the increase in CYTOX, indicating changes in mitochondrial composition. Hypothyroidism reduced cytochrome c in muscle by 30-35% at 56 days, but had no effect in heart, indicating a muscle type-specific effect of thyroid hormone on cytochrome c protein expression. Cytochrome c mRNA increased rapidly to 4-5 fold above the fetal level in both heart and muscle by 6 h post-partum. Between 7 and 56 days of age, further increases to 6- and 25-fold were observed in muscle and heart, respectively. In muscle, the 6-fold developmental increase in mRNA paralleled that of the protein, suggesting transcriptional regulation.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2006

Revealing the complementation of ferredoxin by cytochrome b (5) in the Spirulina- (6)-desaturation reaction by N-terminal fusion and co-expression of the fungal-cytochrome b (5) domain and Spirulina- (6)-acyl-lipid desaturase.

Spirulina-acyl-lipid desaturases are integral membrane proteins found in thylakoid and plasma membranes. These enzymes catalyze the fatty acid desaturation process of Spirulina to yield gamma-linolenic acid (GLA) as the final desaturation product. It has been reported that the cyanobacterial desaturases use ferredoxin as an electron donor, whereas the acyl-lipid desaturase in plant cytoplasm and the acyl-CoA desaturase of animals and fungi use cytochrome b (5). The low level of ferredoxin present in Escherichia coli cells leads to an inability to synthesize GLA when the cells are transformed with the Spirulina-(6) desaturase, desD, and grown in the presence of the reaction substrate, linoleic acid. In this study, Spirulina-(6) desaturase, encoded by the desD gene, was N-terminally fused and co-expressed with the cytochrome b (5) domain from Mucor rouxii. The product, GLA, made heterologously in E. coli and Saccharomyces cerevisiae, was then detected and analyzed. The results revealed the production of GLA by Spirulina-(6) desaturase fused or co-expressed with cytochrome b (5) in E. coli cells, in which GLA production by this gene cannot occur in the absence of cytochrome b (5). Moreover, the GLA production ability in the E. coli host cells was lost after the single substitution mutation was introduced to H52 in the HPGG motif of the cytochrome b (5) domain. These results revealed the complementation of the ferredoxin requirement by the fusion or co-expression of the fungal-cytochrome b (5) domain in the desaturation process of Spirulina-(6) desaturase. Furthermore, the free form of cytochrome b (5) domain can also enhance GLA production by the Spirulina-desD gene in yeast cells.

Amino Acid Motifs↗
PubMed2005

A structural model for the adduct between cytochrome c and cytochrome c oxidase.

An ensemble of structural models of the adduct between cytochrome c and cytochrome c oxidase from Paracoccus denitrificans has been calculated based on the experimental data from site-directed mutagenesis and NMR experiments that have accumulated over the last years of research on this system. The residues from each protein that are at the protein-protein interface have been identified by the above experimental work, and this information has been converted in a series of restraints explicitly used in calculations. It is found that a single static structural model cannot satisfy all experimental data simultaneously. Therefore, it is proposed that the adduct exists as a dynamic ensemble of different orientations in equilibrium, and may be represented by a combination or average of the various limiting conformations calculated here. The equilibrium involves both conformations that are competent for electron transfer and conformations that are not. Long-range recognition of the partners is driven by non-specific electrostatic interactions, while at shorter distances hydrophobic contacts tune the reciprocal orientation. Electron transfer from cytochrome bc (1) to cytochrome c oxidase is mediated through cytochrome c experiencing multiple encounters with both of its partners, only part of which are productive. The number of encounters, and thus the electron transfer rate, may be increased by the formation of a cytochrome bc (1)-cytochrome c oxidase supercomplex and/or (in human) by increasing the concentration of the two enzymes in the membrane space.

Cytochromes c↗
PubMed1999

Nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774:primary sequence determination, crystallographic refinement at 1.8 and modelling studies of its interaction with the tetrahaem cytochrome c3.

A monomeric nine-haem cytochrome c (9Hcc) with 292 amino acid residues was isolated from cells of the sulfate- and nitrate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 grown under both nitrate- and sulfate-respiring conditions. The nucleotide sequence encoding the 292 residues was determined, allowing the correction of about 10% of the previous primary structure, determined from 1.8 A electron density maps. The refinement at 1.8 A resolution of the structural model was completed, giving an R-value of 16.5%. The nine haem groups are arranged into two tetrahaem clusters, located at both ends of the molecule, with Fe-Fe distances and local protein fold very similar to tetrahaem cytochromes c3, and the extra haem is located asymmetrically between the two regions. The new primary sequence determination confirmed the 39% sequence homology found between this cytochrome and the C-terminal region (residues 229-514) of the high-molecular-weight cytochrome c (Hmc) from D. vulgaris Hildenborough, providing strong evidence of structural similarity between 9Hcc and the C-terminal region of Hmc. The interaction between 9Hcc and the tetrahaem cytochrome c3 from the same organism was studied by modelling methods, and the results suggest that a specific interaction is possible between haem 4 of tetrahaem cytochrome c3 and haem 1 or haem 2 of 9Hcc, in agreement with previous kinetic experiments which showed the catalytic effect of the tetrahaem cytochrome c3 upon the reduction of 9Hcc by the [NiFe] hydrogenase from D. desulfuricans ATCC 27774. These studies suggest a role for 9Hcc as part of the assembly of redox proteins involved in recycling the molecular hydrogen released by the cell as a result of substrate oxidation.

Amino Acid Sequence↗
PubMed1984

Kinetics of cytochrome c and TMPD oxidation by cytochrome c oxidase from the thermophilic bacterium, PS3.

Cytochrome caa3 (cytochrome oxidase) from the thermophilic bacterium PS3 can exhibit full catalytic activity in the presence of ascorbate and TMPD or other electron donors and in the absence of added soluble c-type cytochromes. It appears to possess only a low-affinity and not a high-affinity site for the soluble cytochromes. Proteoliposomal cytochrome caa3 develops an effective membrane potential in the presence of ascorbate and TMPD or PMS, in the absence of added soluble cytochrome c. Reduction of the a3 centre is blocked in the presence of cyanide. During reductive titrations of the cyanide-inhibited enzyme, electrons initially equilibrate among three centres, the c haem, the a haem and one of the associated Cu atoms. During steady-state turnover, electrons probably enter the complex via the bound c haem; the a haem and perhaps an associated CuA atom are reduced next. It is concluded that, despite its size and hydrophobic association with the aa3 complex, the haem c-containing subunit can behave in an analogous way to that of mammalian cytochrome c, bound at the high-affinity site of the eucaryotic enzyme.

Bacteria↗
PubMed1981

Transglutaminase-catalysed incorporation of putrescine into denatured cytochrome. Preparation of a mono-substituted derivative reactive with cytochrome c oxidase.

Guinea pig liver transglutaminase has been used to incorporate putrescine into horse heart cytochrome c. The native protein showed essentially no incorporation, while ethanol-denatured cytochrome c incorporated almost 1 mol putrescine per mol protein. No increase in this level of modification was obtained when maleylated cytochrome c and the tryptic peptides of cytochrome c were used as substrates. Analysis of the modified ethanol-denatured cytochrome c by tryptic cleavage and peptide isolation showed that glutamine-42 of the intact protein is the site of incorporation of radioactively labelled putrescine. Ethanol-denatured cytochrome c that was specifically modified at glutamine-42 by incorporated of putrescine could be readily renatured. The renatured modified protein showed reactivity with cytochrome c oxidase comparable to that of the original native protein.

Animals↗
PubMed1983

Interaction between cytochrome c and ubiquinone-cytochrome c oxidoreductase: a study with water-soluble carbodiimides.

The role of carboxyl groups on the interaction between ubiquinone-cytochrome c oxidoreductase (Complex III) and cytochrome c has been probed using the two water-soluble carbodiimides EDC (1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide) and CMC (1-cyclohexyl-3-(2-morpholinyl-4-ethyl) carbodiimide metho-p-toluensulphonate). The results suggest that: 1) carboxyl groups present on both cytochrome c1 and subunit VIII are modified. Some of these residues are shielded by cytochrome c. 2) The enzyme activity decreases during the carbodiimide treatment and the extent of inhibition is larger in the presence of cytochrome c. 3) Cytochrome c, equimolar with the enzyme, cross-links to cytochrome c1 and subunit VIII via the carbodiimide-activated carboxyl groups. The two subunits appear to be in contact in the isolated enzyme.

Animals↗
PubMed1983

Characterization of cytochrome b in the isolated ubiquinol-cytochrome c2 oxidoreductase from Rhodopseudomonas sphaeroides GA.

Extinction coefficients for cytochrome b and c1 in the isolated cytochrome bc1 complex from Rhodopseudomonas sphaeroides GA have been determined. They are 25 mM-1 . cm-1 at 561 nm for cytochrome b and 17.4 mM-1 . cm-1 at 553 nM for cytochrome c1, for the difference between the reduced and the oxidized state. Cytochrome b is present in two forms in the complex. One form has an Em7 of 50 mV, an alpha-peak of 557 nm at liquid N2 temperature and of 561 nm at RT, which is red-shifted by antimycin A. The other form has an Em7 of -90 mV, a double alpha-peak of 555 and 561 nm at liquid N2 temperature corresponding to 559 and 566 nm at RT. The absorption at 566 nm is red-shifted by myxothiazol. The two shifts are independent of each other. Both midpoint potentials of cytochromes b are pH-dependent. The redox center compositions of the cytochrome bc1 complexes from Rhodopseudomonas sphaeroides and from mitochondria are identical.

Antimycin A↗
PubMed1985

Cytochrome P450 of small intestinal epithelial cells. Immunochemical characterization of the increase in cytochrome P450 caused by phenobarbital.

We have studied total cytochrome P450 and the major form of cytochrome P450 increased by phenobarbital in small intestinal epithelial cells and livers of male Sprague-Dawley rats. Using an improved method for preparing microsomes from intestinal epithelial cells, we find that concentrations of total cytochrome P450 in intestinal cell microsomes are 10% of those in liver microsomes, and that this percentage is unchanged after phenobarbital treatment. In untreated rats, less than 5% of total cytochrome P450 of liver or intestinal epithelium is the form induced by phenobarbital, as measured by rocket immunoelectrophoresis. In phenobarbital-treated rats, the major phenobarbital-induced form accounts for approximately 50% of the total in both organs. In the small intestine of phenobarbital-treated rats, the concentrations of total cytochrome P450 and of the major phenobarbital-induced form increase concurrently as epithelial cells mature from crypt to upper villus. Concentrations of total cytochrome P450 and of the major phenobarbital-induced form in the proximal two-thirds of the rat small intestine are twofold higher than in the distal third. Immunoblotting performed with a monoclonal antibody to the major phenobarbital-induced form of cytochrome P450 from rat liver revealed a subtle difference between this form in liver and intestine.

Animals↗
PubMed1995

Beta-thiopropionyl cytochromes c modified at lysyl residues: preparation and characterization of the monosubstituted horse cytochromes c.

beta-Thiopropionyl derivatives of horse cytochrome c singly modified at each of 18 different lysine epsilon-amino groups have been prepared using sulfosuccinimidyl-2-(biotinamido)ethyl-1,3-dithiopropionate and purified to homogeneity by high-pressure liquid chromatography. These derivatives were characterized by determination of: (i) the location of the modification; (ii) reduction potentials; (iii) visible and NMR spectra: and by (iv) measurement of electron transfer activity with cytochrome-c oxidase. No significant changes in structure were indicated, except for the ferric forms of the derivatives modified at lysines 72, 73, and 79 which are discussed separately. The electron transfer activity of the beta-thiopropionyl cytochromes c with bovine heart cytochrome-c oxidase was decreased to extents dependent on the position of the modification. Aminoethylation, a secondary modification which reverses the charge change, restored the electron transfer rate to that observed with the unmodified cytochrome c, irrespective of the location of the primary modification. These results afford a direct experimental demonstration that alterations in kinetics with physiological electron transfer partners resulting from modifications which cause a change of the charge of surface side chains are solely due to the electrostatic effects. Of the many chemically modified cytochromes c prepared to date, the singly substituted beta-thiopropionyl cytochromes c are likely to be particularly useful as the thiol allows covalent linkage of any sulfhydryl-reactive reagent to a well-defined location on the protein surface by a simple procedure, even when the secondary modifier is relatively unstable, a crucial advantage not otherwise readily achieved.

Amino Acid Sequence↗
PubMed1977

Immunoassay for honey bee cytochrome c in single animals with cytochrome c-coated bacteriophages: a sensitive tool for the study of caste formation in the honey bee, Apis mellifera.

The development of a sensitive viroimmunoassay for honey bee cytochrome c and its usage for early detection of caste differentiation is described. Pure honey bee cytochrome c was isolated from workers and used to produce antibodies in rabbits. Bacteriophage T4 was chemically modified by covalent attachment of honey bee cytochrome c using tolylene-2,4-diisocyanate as a cross-linking agent. The immunospecific inactivation of this bacteriophage-cytochrome c conjugate by anti-cytochrome c antibodies can be inhibited by free cytochrome c. In quantitative determinations, 50% inhibition is reproducibly achieved at a concentration of 6 ng/ml (5 pmol/ml) and as little as 0.3 ng/ml (0.25 pmol/ml) could be detected by this system. Cytochrome c concentrations were measured in individual animals and substantial differences corresponding larval stages of worker and queen bees are reported.

Antibodies↗