Amino acid sequence of a ferredoxin from Rhodymenia palmata, a red alga in the florideophyceae

The amino acid sequence of a [2Fe-2S] ferredoxin from a red alga, Rhodymenia palmata in the family Florideophyceae, was determined by conventional methods. The ferredoxin is composed of 97 amino acid residues having five cysteines, but lacking methionine and tryptophan. It possesses a number of structural features of particular interest. The amino acid sequence is compared with those previously determined for ferredoxins from two red algae in the family Bangiophyceae. Conclusions from a comparison of the structures, by noting features such as the presence of gaps in the sequences and by constructing a phylogenetic tree, were consistent with the proposed taxonomic relationship among these algae.     

Amino acid sequence of ferredoxin from Arctium lappa

Ferredoxin from Arctium lappa consists of a single polypeptide chain of 97 residues, four of which are cysteine. These residues, which are in the active centre, are in identical positions to those of other ferredoxins. Overlap between residue positions 50/51 was not obtained, but amino acid composition of the two cyanogen bromide fragments which were overlapped corresponded with the amino acid composition of the total protein.     

The amino acid sequence of ferredoxin from Sambucus nigra

The amino acid sequence of the ferredoxin from Sambucus nigra consists of a single polypeptide chain of 97 amino acid residues, 5 of which are cysteine. The positions of the 4 cysteine residues which bind the iron atoms of the active centre are identical to those of other ferredoxins. Due to difficulties of obtaining pure protein, residues 87–90 have only been identified from the amino acid analysis of peptide C 10 and by homology with other higher plant ferredoxins.     

Cytochrome cs from Rhodymenia palmata and Porphyra umbilicalis and the amino acid sequences of their N-terminal regions

Basic c-type cytochromes homologous with plant and animal mitochondrial cytochrome c have been isolated and purified from Rhodymenia palmata and Porphyra umbilicalis. The N-terminal regions have been analysed using a Beckman 890C automatic sequencer. When compared to animal cytochrome c, the Rhodymenia cytochrome c has an unblocked N-terminal tail of 10 amino acids, whereas Porphyra has an unblocked N-terminal tail of only a single amino acid.     

Comparative properties of ferredoxins from a marine and freshwater species of Porphyridium

Ferredoxins were isolated from the freshwater red alga Porphyridium aerugineut, and from Porphyridium cruentum, a related marine species. A sin     

Isolation and properties of a ferredoxin from Anabaena Flos-Aquae

Ferredoxin was isolated from the blue-green alga Anabaena flos-aquae. Its homogeneity was shown by conventional and SDS-polyacrylamide gel electrophoresis, and isoelectric focusing on polyacrylamide gel columns, the latter indicating a pI at ca pH 3·7. The absorption spectrum had, in the oxidized state, maxima at 462, 421, 327 and 276 nm, with a shoulder at 284 nm, a spectrum characteristic of plant-type ferredoxins. The 421 : 276 nm absorbance ratio was typically 0.49. The ferredoxin effectively mediated the photoreduction of NADP⁺ by barley chloroplasts depleted of native ferredoxin. The MW obtained by sedimentation-equilibrium and sedimentation velocity-diffusion coefficient studies was ca 12 000 daltons, a value somewhat higher than suggested by amino acid composition data. The ferredoxin contained 2Fe and 2S per molecule.     

Isolation and properties of crystalline ferredoxin from lactuca sativa

Lettuce ferredoxin has been purified to homogeneity, with a yield of 18 mg/kg of denerved leaves. It crystallizes in magnificent needles, often clustered in broom-like sheaves. The absorption spectrum showed maxima at 460, 422, 330 and 274 nm,with a ratio A₄₂₂/A₂₇₄, of 0.46. The mM absorption coefficient was 9.74 at 422 nm, and 21.62 at 274 nm. This ferredoxin showed a pI = 4.7 and an E′₀ = ?425 mV (at pH = 7.7). MWs of 12 400, 11480 and 13000 were obtained by sucrose gradient centrifugation, and on the basis of the amino acid composition and the iron content, respectively, with an average of 12 300. The amino acid analysis showed the existence of one methionine residue per mole, with 105 amino acid residues. There are two iron atoms and two labile sulfide groups per mole; 4 half-cystine residues were found by performic acid oxidation, and 5 cysteine groups when determined by titration with pHMB. The native protein is not fixed on thiol-Sepharose 4B, but it is quantitatively retained after incubation with 8 M urea. Lettuce ferredoxin showed a 62, 58 and 78% effectiveness with the spinach ferredoxin-NADP reductase, nitrite reductase and fructose-1,6-diphosphatase (FDPase), respectively, when compared with the spinach ferredoxin. This different behaviour of both ferredoxins is joined to genetic-structural relationships, and suggests that the role of ferredoxin in FDPase activation is more sophisticated than that of a mere nonspecific reductant.     

The amino acid sequence of ferredoxin from the alga Mastigocladuslaminosus

Ferredoxin was purified from the thermophilic blue-green alga, Mastigocladuslaminosus. The physicochemical properties of this ferredoxin are similar to those of other [2Fe-2S] plant ferredoxins except for its unusual thermal stability. The primary structure of the protein was determined and consists of 98 amino acid residues, 5 of which are cysteines. The positions of 4 cysteines which bind the iron atoms of the active centre are identical to those in other ferredoxins. The primary structure of the ferredoxin does not reveal any special features to account for its high thermal stability.     

Thermal properties of NADP:ferredoxin oxidoreductase and ferredoxin isolated from a thermophilic blue-green alga

NADP:ferredoxin oxidoreductase (EC. 1.6.7.1.) isolated from a thermophilic blue-green alga, Synechococcus sp., was stable at temperatures up to 65°C. The diaphorase and cytochrome c reductase activities of the enzyme were low at 25°C but increased with elevated temperature to reach a maximum at about 60°C. The pH-profile of the diaphorase activity showed a peak at pH 9.0 at 55°C, whereas the activity was largely independent of pH at 25°C. High concentrations of NaCl suppressed activity at both high and low temperatures. In the cytochrome c reductase activity catalyzed by the enzyme, ferredoxin served as an electron carrier in a temperature-insensitive manner over a wide range of temperature. The results support the view that the optimum and the upper limiting temperatures for photosynthesis in this alga are related to thermal properties of proteins.     

The amino acid sequence of cytochrome c from niger-seed, Guizotia abyssinica

The amino acid sequence of cytochrome c from niger-seed has been determined by sequence analysis of chymotryptic and tryptic peptides using the dansyl-phenylisothiocyanate method and by qualitative analysis of peptide composition by the dansyl method. Although the spectral ratios indicated the protein was not completely pure, no indication of impurity was found during the sequence analysis and no peptides in addition to those given here were obtained. In certain cases the alignment of peptides was by homology with other cytochromes c. Four residues in the proposed sequence, alanine-1, cysteine-25, histidine-26 and lysine-61 were identified only from peptide compositions. The amino-terminus of the protein is acetylated. The sequence contains two residues of ϵ-N-trimethyllysine.     

Sterols of the amansieae (rhodomelaceae: Rhodophyta)

Osmundaria prolifera, kuetzingia natalensis, Halopythis pinastroïdes and Vidalia fimbriata contain C₂₇ sterols as the major sterols. Six other species of the Amansieae, belonging to the genera Amansia, Vidalia, Lenormandia and Rythiphlaea, contain C₂₈-sterols as the major sterols.     

The amino acid sequences of plastocyanin from Mercurialis perennis and Capsella bursa-pastoris

The amino acid sequences of the plastocyanins from Mercurialis perennis and Capsella bursa-pastoris have been determined. The amides at positions 64 and 68 in the Mercurialis sequence were positioned by ‘homology’ Both proteins are single polypeptide chains of 99 residues and are closely related to other higher plant plastocyanins.     

The amino acid sequence of plastocyanin from Cucumis sativus

The amino acid sequence of plastocyanin from cucumber (Cucumis sativus) has been determined. Analysis was by the dansyl—phenylisothiocyanate meth     

The amino acid sequence of plastocyanin from Rumex obtusifolius

The amino acid sequence of plastocyanin from dock has been completed. It is a single polypeptide chain of 99 residues which is closely related to other plant plastocyanins. Compared to a preliminary sequence presented earlier, the completed sequence now shows two changes, at positions 53 and 92.     

Composition of Gigartina carrageenan in relation to sporophyte and gametophyte stages of the life cycle

Total carrageenan levels (55–88% of plant dry weight) of four Gigartina species showed little variation between male, female and tetrasporic plants. However whereas male and female gametophyte plants gave carrageenans with K: λ ratios usually ranging from 1·0 to 4·0, with one species in the range 0·3–0·8, tetrasporophyte carrageenans gave very low K: λ ratios, 0·02–0·1, indicative of a virtual absence of K-carrageenan from plants of this stage of the life cycle.     

Primary structure of ferredoxin from bovine kidney mitochondria

Kidney mitochondrial ferredoxin (renodoxin) is a component of the cytochrome P-450-dependent enzymatic system whose main function is the hydroxylation of vitamin D₃ in the 1a- and 24-positions. The complete amino acid sequence of renodoxin was determined by protein chemistry and mass spectrometry. The mature renodoxin has 128 amino acid residues. The N- and C-terminal regions of renodoxin are subject to proteolytic modification, this being the origin of heterogeneous molecular mass (from 14,200 to 12,400 kD) of purified protein preparations. The antigenic structure of renodoxin was studied using antibodies to peptide fragments of a homologous protein, adrenodoxin.     

The amino acid sequence of plastocyanin from Lactuca sativa (lettuce)

The amino acid sequence of plastocyanin from lettuce (Lactuca sativa L.) was determined by using a Beckman 890C automatic sequencer and by dansyl-phenylisothiocyanate analysis of peptides obtained by enzymic digestion of purified CNBr fragments. The protein consists of a single polypeptide chain of 99 residues, and shows close homology with other higher plant plastocyanins. The data are discussed in relation to the possible residues involved in the binding of copper in plastocyanin.     

Amino acids and low-molecular-weight carbohydrates of some marine red algae

Amino acids and low-MW carbohydrates of 18 red algae have been analyzed. Several non-protein amino acids have been identified, including pyrrolidine-2,5-dicarboxylic acid (3c) and N-methylmethionine sulfoxide (5), new natural products, and 13 known compounds, citrulline, β-alanine, γ-aminobutyric acid, baikiain (1), pipecolic acid (2), domoic acid (3a), kainic acid (3b), azetidine-2-carboxylic acid (4), methionine sulfoxide taurine, N-methyltaurine, N,N-dimethyltaurine and N,N,N-trimethyltaurine. Sugars present were mainly floridoside, isofloridoside and mannoglyceric acid. Details of the structural elucidation of new compounds are also given.