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PubMed1978

Isolation and characterization of a membrane-bound, low-potential c-type cytochrome from purple photosynthetic bacteria, with special reference to Rhodospirillum rubrum.

Other investigators have isolated soluble, low-potential, c-type cytochromes (cytochrome c3) from a few photosynthetic procaryotes, i.e., a cyanobacterium and two species of purple nonsulfur bacteria. However, such cytochromes appeared to be absent from other purple bacteria, including Rhodospirillum rubrum and Chromatium vinosum. We now report evidence for the presence of low-potential c-type cytochromes in these two species, in which they were found to be bound to the photosynthetic membranes. Evidence for a membrane-bound, low-potential c-type cytochrome was also found in Rhodopseudomonas sphaeoides. The low-potential c-type cytochrome of R. rubrum was solubilized by a Triton X-100 treatment of chromatophores and was partly purified. It was found to have a molecular weight of about 17,000, a midpoint oxidation-reduction potential of -192 mV, and an alpha-absorption peak at 552 nm. It appears that low-potential c-type cytochromes may be present in all purple photosynthetic bacteria, of both the sulfur and the nonsulfur types.

Bacterial Proteins↗
PubMed1979

Two forms of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum.

Acetylene reduction by nitrogenase from Rhodospirillum rubrum, unlike that by other nitrogenases, was recently found by other investigators to require an activation of the iron protein of nitrogenase by an activating system comprising a chromatophore membrane component, adenosine 5'-triphosphate (ATP), and divalent metal ions. In an extension of this work, we observed that the same activating system was also required for nitrogenase-linked H(2) evolution. However, we found that, depending on their nitrogen nutrition regime, R. rubrum cells produced two forms of nitrogenase that differed in their Fe protein components. Cells whose nitrogen supply was totally exhausted before harvest yielded predominantly a form of nitrogenase (A) whose enzymatic activity was not governed by the activating system, whereas cells supplied up to harvest time with N(2) or glutamate yielded predominantly a form of nitrogenase (R) whose enzymatic activity was regulated by the activating system. An unexpected finding was the rapid (less than 10 min in some cases) intracellular conversion of nitrogenase A to nitrogenase R brought about by the addition to nitrogen-starved cells of glutamine, asparagine, or, particularly, ammonia. This finding suggests that mechanisms other than de novo protein synthesis were involved in the conversion of nitrogenase A to the R form. The molecular weights of the Fe protein and Mo-Fe protein components from nitrogenases A and R were the same. However, nitrogenase A appeared to be larger in size, because it had more Fe protein units per Mo-Fe protein than did nitrogenase R. A distinguishing property of the Fe protein from nitrogenase R was its ATP requirement. When combined with the Mo-Fe protein (from either nitrogenase A or nitrogenase R), the R form of Fe protein required a lower ATP concentration but bound or utilized more ATP molecules during acetylene reduction than did the A form of Fe protein. No differences between the Fe proteins from the two forms of nitrogenase were found in the electron paramagnetic resonance spectrum, midpoint oxidation-reduction potential, or sensitivity to iron chelators.

Acetylene↗
PubMed1979

Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100.

A succinic dehydrogenase (SDH) complex has been purified from Triton X-100-solubilized membranes from Bacillus subtilis by precipitation with specific antibody. Radioactively labeled precipitated complex was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography of the gels. The complex contained equimolar amounts of three polypeptides with approximate molecular weights of 65,000, 28,000, and 19,000. Five succinic dehydrogenase-negative mutants, belonging to the citF group, contained the 65,000-dalton polypeptide in a soluble form in the cytoplasm. Each 65,000-dalton polypeptide had about one molecule of flavin bound. Another citF mutant, citF11, which lacks the 65,000-dalton polypeptide, contained a membrane-bound 28,000-dalton polypeptide. The wild-type succinic dehydrogenase complex contained cytochrome, probably a cytochrome b. The 19,000-dalton polypeptide is suggested to represent the apoprotein of this cytochrome. The 65,000-dalton and the 28,000-dalton polypeptides are thought to constitute succinic dehydrogenase and to correspond to the flavoprotein and the ironprotein, respectively, as described for succinic dehydrogenase isolated from beef heart mitochondria or Rhodospirillum rubrum chromatophores. The results presented suggest that in B. subtilis succinic dehydrogenase is attached to a cytochrome b in the membrane via the 28,000-dalton (ironprotein) polypeptide.

Bacillus subtilis↗
PubMed1982

Nitrate reductase from Rhodopseudomonas sphaeroides.

The facultative phototroph Rhodopseudomonas sphaeroides DSM158 was incapable of either assimilating or dissimilating nitrate, although the organism could reduce it enzymatically to nitrite either anaerobically in the light or aerobically in the dark. Reduction of nitrate was mediated by a nitrate reductase bound to chromatophores that could be easily solubilized and functioned with chemically reduced viologens or photochemically reduced flavins as electron donors. The enzyme was solubilized, and some of its kinetic and molecular parameters were determined. It seemed to be nonadaptive, ammonia did not repress its synthesis, and its activity underwent a rapid decline when the cells entered the stationary growth phase. Studies with inhibitors and with metal antagonists indicated that molybdenum and possibly iron participate in the enzymatic reduction of nitrate. The conjectural significance of this nitrate reductase in phototrophic bacteria is discussed.

Iron↗
PubMed1983

Isolation and characterization of enhanced fluorescence mutants of Rhodopseudomonas capsulata.

After enrichment by a tetracycline suicide under conditions nonpermissive for the growth of mutants defective in photosynthesis, colonies were screened for enhanced fluorescence in near-infrared light by using high-speed infrared photography. Twenty mutants were isolated, and the chromatophore membranes were analyzed by a new, rapid microprocedure that revealed many different phenotypes among the mutants. The enhanced fluorescence mutants typically possessed a functional light-harvesting II antenna, but showed reduced or absent light-harvesting I. Twelve isolates were also defective in reaction center polypeptides. An R-prime plasmid that bears 50 kilobases of Rhodopseudomonas capsulata DNA coding for components of the photosynthetic apparatus (B. L. Marrs, J. Bacteriol. 146:1003-1012, 1981), pRPS404, complemented all 20 enhanced fluorescence mutants as demonstrated by the quenching of fluorescence in mutants that had received the R-prime plasmid by conjugation. Fluorescence was regained upon loss of the 50-kilobase insert. Complementation of the fluorescent lesions implies that most or all of the genes necessary for the expression of the reaction center and the light-harvesting antennae are carried by the R-prime plasmid and that these genes are actively transcribed in the homologous organism. All 20 mutants are complemented by one of two pBR322 subclones of the R-prime plasmid, pRPSEB2 or pRPSE2. pRPSEB2 bears a 4.5-kilobase fragment of R. capsulata DNA including the rxcA locus, and pRPSE2 is a pBR322 derivative bearing a 7.5-kilobase R. capsulata DNA fragment bearing the rxcB locus. These fragments therefore carry sequences necessary for the normal synthesis of the light-harvesting and reaction center polypeptide complexes.

Bacterial Proteins↗
PubMed1987

Cell-cycle-specific fluctuation in cytoplasmic membrane composition in aerobically grown Rhodospirillum rubrum.

Aerobic growth with synchronous cell division was induced in Rhodospirillum rubrum by starvation methods. Cells were harvested at different points in the cell cycle. Analysis of the composition of the cell envelope prepared by differential centrifugation or density gradient-purified cytoplasmic membrane obtained from cells at different times indicated that the protein/phospholipid ratio fluctuated with the cell cycle. The protein/phospholipid ratio of cell envelope from selection-synchronized cells also fluctuated with the cell cycle. These studies indicate that the phenomenon of cell-cycle-dependent fluctuation in membrane composition is not restricted to the intracytoplasmic chromatophore membrane of phototrophic cells.

Aerobiosis↗
PubMed1991

Construction, characterization, and complementation of Rhodospirillum rubrum puf region mutants.

Rhodospirillum rubrum is a facultatively phototrophic bacterium that, under certain growth conditions, forms an intracytoplasmic chromatophore membrane (ICM) housing the photochemical apparatus. The puf operon of R. rubrum encodes protein subunits of the photochemical reaction center and the B880 light-harvesting antenna complex. Mutant strains of R. rubrum were constructed by interposon mutagenesis through which a kanamycin resistance gene cartridge was inserted into restriction sites and in place of restriction fragments of the puf region. Southern blot analysis demonstrated that the defective copies of puf sequences had replaced their normal chromosomal counterparts through homologous recombination. The phenotypes of the mutant strains were evaluated on the basis of puf gene expression, spectral analysis, pigment content of membranes, and electron-microscopic examination of thin sections of cells grown under semi-aerobic and dark anaerobic conditions. Alterations of the puf region affect phototrophic competence and the formation of the ICM. The latter result implies an obligatory role for puf gene products in ICM formation in R. rubrum. One mutant with a deletion in puf structural genes was complemented in trans to the wild-type phenotype. Other mutants could be restored to the wild-type phenotype only by recombination.

Blotting, Northern↗
PubMed1992

Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides.

It has recently become evident that many bacterial respiratory oxidases are members of a superfamily that is related to the eukaryotic cytochrome c oxidase. These oxidases catalyze the reduction of oxygen to water at a heme-copper binuclear center. Fourier transform infrared (FTIR) spectroscopy has been used to examine the heme-copper-containing respiratory oxidases of Rhodobacter sphaeroides Ga. This technique monitors the stretching frequency of CO bound at the oxygen binding site and can be used to characterize the oxidases in situ with membrane preparations. Oxidases that have a heme-copper binuclear center are recognizable by FTIR spectroscopy because the bound CO moves from the heme iron to the nearby copper upon photolysis at low temperature, where it exhibits a diagnostic spectrum. The FTIR spectra indicate that the binuclear center of the R. sphaeroides aa3-type cytochrome c oxidase is remarkably similar to that of the bovine mitochondrial oxidase. Upon deletion of the ctaD gene, encoding subunit I of the aa3-type oxidase, substantial cytochrome c oxidase remains in the membranes of aerobically grown R. sphaeroides. This correlates with a second wild-type R. sphaeroides is grown photosynthetically, the chromatophore membranes lack the aa3-type oxidase but have this second heme-copper oxidase. Subunit I of the heme-copper oxidase superfamily contains the binuclear center. Amino acid sequence alignments show that this subunit is structurally very highly conserved among both eukaryotic and prokaryotic species. The polymerase chain reaction was used to show that the chromosome of R. sphaeroides contains at least one other gene that is a homolog of ctaD, the gene encoding subunit I of the aa3-type cytochrome c oxidase.(ABSTRACT TRUNCATED AT 250 WORDS)

Base Sequence↗
PubMed1995

Mutation of the Ser2 codon of the light-harvesting B870 alpha polypeptide of Rhodobacter capsulatus partially suppresses the pufX phenotype.

The exact function of the pufX gene product of Rhodobacter capsulatus is uncertain, but deletion of the pufX gene renders cells incapable of phototrophic growth on a minimal medium, and photosynthetic electron transfer is impaired in vitro. However, suppressor mutants that are able to grow phototropically are readily isolated. Two such suppressor mutants were characterized as to their phototrophic growth properties, their fluorescence at different incident light intensities, the integrity of their chromatophores, and their abilities to generate a transmembrane potential. We found that the photosynthetic apparatus in the suppressor mutants was less stable than that of the pseudo-wild-type and primary mutant strains and that the suppressor mutants used light energy less efficiently than the pseudo-wild-type strain. Therefore, the suppressor strains are more precisely designated partial suppressor mutants. The locations and sequences of the suppressor mutations were determined, and both were found to change the second codon of the pufA gene. It is hypothesized that the serine residue specified by this codon is important in interactions between the B870 alpha protein and other membrane-bound polypeptides and that suppressor mutations at this position partially compensate for loss of the PufX protein. A model is proposed for the function of the PufX protein.

Amino Acid Sequence↗
PubMed1996

Directed mutagenesis of the Rhodobacter capsulatus puhA gene and orf 214: pleiotropic effects on photosynthetic reaction center and light-harvesting 1 complexes.

Rhodobacter capsulatus puhA mutant strains containing either a nonpolar, translationally in-frame deletion or a polar insertion of an antibiotic resistance cartridge were constructed and evaluated for their photosynthetic growth properties, absorption spectroscopy profiles, and chromatophore protein compositions. Both types of mutants were found to be incapable of photosynthetic growth and deficient in the reaction center (RC) and light-harvesting 1 (LH1) complexes. The translationally in-frame puhA deletion strains were restored to the parental strain phenotypes by complementation with a plasmid containing the puhA gene, whereas the polar puhA mutants were not. Analogous nonpolar and polar disruptions of orf 214 (located immediately 3' of the puhA gene) were made, and the resultant mutant strains were evaluated as described above. The strain containing the nonpolar deletion of orf 214 exhibited severely impaired photosynthetic growth properties and had greatly reduced levels of the RC and LH1 complexes. Complementation of this strain with a plasmid that expressed orf 214 from the nifHDK promoter restored photosynthetic growth capability, as well as the RC and LH1 complexes. The polar disruption of orf 214 yielded cells that were incapable of photosynthetic growth and had even lower levels of the RC and LH1 complexes, and complementation in trans with orf 214 only marginally improved these deficiencies. These results indicate that orf 214 and at least one additional gene located 3' of orf 214 are required to obtain the RC and LH1 complexes, and transcription read-through from the puhA superoperon is necessary for optimal expression of these new photosynthesis genes.

Amino Acid Sequence↗
PubMed1986

Structure, partial elemental composition, and size of Thiopedia rosea cells and platelets.

The phototrophic purple sulfur bacterium Thiopedia rosea forms multicellular, gas-vacuolate, regular, flat aggregates (platelets, sheets) held together by slime. Platelets found in eutrophic water consisted of slime (85% of the total wet volume) and 16 cells, while the gas-filled vacuole occupied 44% of the volume of a single wet cell. Individual platelet cells contained central spindle-shaped gas vesicles (which together constitute the cell's gas vacuole), intracytoplasmic membrane vesicles (chromatophores), and peripheral sulfur globules. Cells were surrounded by a Gram-negative type cell envelope and were connected to neighboring cells of the same platelet by mostly unstructured slime. Cells contained detectable amounts of magnesium, phosphorus, sulfur, and potassium as determined by wavelength-dispersive X-ray microanalysis. The large size and relatively low slime density of the platelet, as well as the flat shape, could greatly decrease platelet sedimentation and so stabilize the position of T. rosea within its water column.

Electron Probe Microanalysis↗
PubMed2000

Still looking for the Ivory Tower.

Following graduate training, which was disrupted by my changing schools and serving in the Navy in World War II, I arrived in Berkeley in 1948 as an instructor in the Biochemistry Department. Despite numerous academic reorganizations and a host of struggles over the University-imposed Loyalty Oath, dismissal of a faculty member because of political affiliations, free speech for students, and my resistance to mandatory retirement, I survived with the help of great graduate students, postdoctoral fellows, undergraduates, superb research assistants, and a supportive wife. Studies on structure of tobacco mosaic virus led to our investigating an ultracentrifuge anomaly and the construction of a synthetic boundary cell. In turn, this resulted in about 15 years of research on the ultracentrifuge and its application to the study of biological macromolecules. Among the latter, the discovery of large ribonucleoprotein complexes, now known as ribosomes, and chromatophores in photosynthetic microorganisms attracted the most attention. But it was the development of the photoelectric absorption optical system and the incorporation of the Rayleigh interferometer onto the ultracentrifuge that had the greatest impact on our further research. These tools, when applied to our initial research on E. coli aspartate transcarbamoylase (ATCase), led to the discovery of distinct subunits for catalysis and regulation and the global conformational change in the enzyme associated with its role in regulation. For almost 35 years we have been using the techniques of protein chemistry and molecular biology in studies of structural and conformational changes in the enzyme, the genes encoding the different polypeptides, subunit interactions, and assembly of the enzyme from six catalytic and six regulatory chains. Hybrids constructed from inactive mutants were used to demonstrate shared active sites requiring the joint participation of amino acid residues from adjoining polypeptide chains. ATCase is still being studied as a model for understanding allostery as a regulatory mechanism. Circularly permuted polypeptide chains are being used to study the folding and assembly pathways, and the recently determined crystal structure of the active nonallosteric catalytic subunit has led to new questions regarding the activated form of ATCase.

Aspartate Carbamoyltransferase↗
PubMed2000

Unraveling the patterns of subclinical pheomelanin-enriched facial hyperpigmentation: effect of depigmenting agents.

BACKGROUND: During photoaging, the density of melanin chromatophores is heterogeneous in the epidermis. AIMS: To define the patterns of pheomelanin-enriched melanotic hypermelanosis of the face in phototype II subjects and to assess the effect of depigmenting agents. Azelaic acid and glycolic acid were tested as well as a soy extract, reported to reduce pigmentation through interaction with the protease-activated receptor 2 (PAR-2) of keratinocytes. METHOD: Evaluations were made by image analysis of high magnification pictures obtained by a video camera equipped with an internal ultraviolet-emitting unit (Visioscan((R))). RESULTS: Three patterns of subclinical facial hypermelanosis were recognized including the spotty perifollicular type, the accretive globular type and the elongated type of the sunny side of wrinkles. Azelaic acid and the soy extract led to significant skin lightening after a 3-week treatment. By contrast, glycolic acid showed an inconsistent effect. CONCLUSION: Sensitive fluorescence video recording combined with image analysis represents an advance in the noninvasive assessment of the mottled subclinical skin pigmentation. The depigmenting effect observed with the soy extract indicates that the inhibition of PAR-2 may be a novel way to approach certain pigmentary disorders of the skin.

Facial Dermatoses↗
PubMed1987

Inherited syndrome with corneal snowflake dystrophy, oculocutaneous pigmentary disturbances, pseudoexfoliation and malabsorption. Statistical data of some symptoms.

Corneal endothelial snowflake dystrophy was diagnosed in a child of 12 years as part of an inherited syndrome associated with various oculocutaneous pigmentation disturbances and malabsorption. Altogether 1,173 people were analyzed, 229 with the dystrophy and 944 controls. Snowflake dystrophy was associated with two kinds of intraocular pigment changes: the prevalence rate of green irides was 21.7% and the prevalence rate of large star-shaped chromatophore-like cells attached to the anterior lens capsule, 23.9%. These associations were statistically significant. The youngest people with green irides or pigmented cells were 14 and 15 years, respectively. After 50 years, the prevalence rates of these pigment changes decreased, and this was statistically significant. Snowflake dystrophy was also associated with malabsorption: the prevalence rate of milk intolerance was 37.6%, lactose malabsorption (hypolactasia) 39.0%, and vitamin A or fat malabsorption 23.3%. The associations between snowflake dystrophy, milk intolerance and hypolactasia were statistically significant.

Adolescent↗
PubMed1993

Standardized ultraviolet-A exposure provokes skin reaction in systemic lupus erythematosus.

The immediate, 1 day and 14 days skin reaction was determined in 23 female SLE patients and 23 age-matched controls after standardized exposure to ultraviolet light of the UV-A wavelengths (320-440 nm). Eighteen of the patients and 12 of the controls were photosensitive by history. Eight separate sites on the buttocks were exposed to UV-A light, four sites at doses between 42 and 252 kJ/m2 and four sites with longpass filters (320, 345, 360 and 375 nm). The reactions on test sites were graded by two independent observers unaware of given doses of filter location. All patients and controls reacted with immediate erythema irrespectively of the presence or absence of photosensitivity. After 1 day, 39% of controls and 78% of patients had erythema and the reactions were more pronounced to longwave UV-A light (> 320 nm) in the patients (P < 0.001). After 14 days, six patients, but no control, had persistent erythema (P = 0.04). Interestingly, three of the four patients without anamnestic photosensitivity did not react on days 1 or 14, while the pattern seen in the controls on day 1 was totally unpredictable with regard to reported photosensitivity. These findings strongly suggest that a considerable proportion of SLE patients show pathological skin reactions to physiological doses of longwave UV-A and not only the far more studied shortwave UV-B (290-320 nm). The responsible chromatophore for the UV-A reaction is not known.

Adolescent↗
PubMed2000

Mass spectrometric survey of peptides in cephalopods with an emphasis on the FMRFamide-related peptides.

A matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) survey of the major peptides in the stellar, fin and pallial nerves and the posterior chromatophore lobe of the cephalopods Sepia officinalis, Loligo opalescens and Dosidicus gigas has been performed. Although a large number of putative peptides are distinct among the three species, several molecular masses are conserved. In addition to peptides, characterization of the lipid content of the nerves is reported, and these lipid peaks account for many of the lower molecular masses observed. One conserved set of peaks corresponds to the FMRFamide-related peptides (FRPs). The Loligo opalescens FMRFa gene has been sequenced. It encodes a 331 amino acid residue prohormone that is processed into 14 FRPs, which are both predicted by the nucleotide sequence and confirmed by MALDI MS. The FRPs predicted by this gene (FMRFa, FLRFa/FIRFa and ALSGDAFLRFa) are observed in all three species, indicating that members of this peptide family are highly conserved across cephalopods.

Amino Acid Sequence↗
PubMed1993

Non-invasive monitoring of the redox state of cytochrome oxidase in living tissue using near-infrared laser lights.

A triple wavelength spectrophotometric method was developed to monitor changes in the concentrations of oxygenated and deoxygenated hemoglobin, and in the redox state of cytochrome oxidase in living tissue. Three wavelengths of an NIR (near-infrared) laser beam were used to monitor hemoglobin (780, 805 and 830 nm) and cytochrome (cyt.) oxidase (780, 790 and 830 nm). Algorithms for calculating changes in the concentrations of oxidized cyt. oxidase (aa3), and oxygenated and deoxygenated hemoglobin were developed using NIR spectral analysis of these chromatophores. To assess the ability of these algorithms to measure independent changes in the concentration of oxy-, deoxyhemoglobin and oxidized cyt. oxidase in tissue, experiments involving a fluorocarbon (FC-43) exchange transfusion at very low hematocrits were conducted in anesthetized rats. The observed data indicate that FC-43 circulation at FiO2 1.0 can supply sufficient oxygen to the rat brain to maintain the oxidation state of mitochondrial oxidase (cyt.aa3) near pre-exchange levels. The relationships between changes in oxidized cyt. oxidase and oxyhemoglobin content in response to variations in FiO2 of inspired gas were then examined in the rat brain. These results also confirmed the ability of the triple wavelength algorithms to distinguish changes in the oxidized copper band of cyt.aa3 from those in absorption by oxy- and deoxyhemoglobin. NIR monitoring of skeletal muscle to determine the redox state of cyt. oxidase was performed in a few human cases and the results indicated that these observations can increase our understanding of the process of oxygen transport to tissues.

Algorithms↗
PubMed2002

Enhancement of hydrogen production by a photosynthetic bacterium mutant with reduced pigment.

A novel mutant MTP4 was created from the wild-type strain Rhodobacter sphaeroides RV by UV irradiation for the enhancement of hydrogen production. The amount of light absorbed by MTP4 was lower than that by the wild-type strain at any wavelengths ranging from 350 to 1000 nm. This nature enables the illumination of cells in the deeper parts of a reactor. The contents of bacteriochlorophylls and carotenoids of the chromatophores prepared from MTP4 under the conditions for hydrogen production were reduced to 41 and 49% of those from the wild-type strain RV, respectively. Analysis of the light-harvesting (LH) complexes by SDS-PAGE showed that the amounts of LH1s and reaction centers (RCs) in MTP4 were retained, whereas that of LH2s was much less than that in RV. Although MTP4 had less pigments, its growth rate was equivalent to that of RV over a wide range of light intensities. MTP4 produces hydrogen with a stable manner. Using a plate-type reactor, it produced 50% more hydrogen than RV. A novel method of pigment reduction was found to be effective for the enhancement of hydrogen production per unit reactor.

Journal Article↗