| isoprenoid quinones in the classification of coryneform and related bacteria. | menaquinones were the only isoprenoid quinones found in 85 of the 95 coryneform bacteria examined. dihydromenaquinones having nine isoprene units were the main components isolated from corynebacterium bovis, from other glutamic acid-producing strains, and from arthrobacter globiformis and related species. dihydromenaquinones with eight isoprene units were found in brevibacterium linens, the remaining corynebacterium species and strains probably belonging to the genus rhodococcus. tetrahydromenaq ... | 1979 | 107269 |
| synthesis of 3'-c-methyladenosine and 3'-c-methyluridine diphosphates and their interaction with the ribonucleoside diphosphate reductase from corynebacterium nephridii. | two nucleoside diphosphate analogs, 3'-c-methyl-adp and 3'-c-methyl-udp, have been tested as substrate and/or allosteric effectors using the adenosylcobalamin-dependent ribonucleoside diphosphate reductase of corynebacterium nephridii. neither analog was a substrate for the reductase. however, they did function as allosteric effectors and as inhibitors of the reduction of adp and udp, respectively. the nucleotide analogs did not stimulate the hydrogen exchange reaction between [5'-3h2]adenosylco ... | 1992 | 1445860 |
| the purification, characterization, and primary structure of a small redox protein from methanobacterium thermoautotrophicum, an archaebacterium. | a small redox-active protein has been purified to homogeneity from cell-free extracts of the strictly anaerobic thermophilic methanogen, methanobacterium thermoautotrophicum (strain marburg). the purification consisted of streptomycin sulfate and acid treatments and three chromatographic steps using sephadex g-75, mono q hr 10/10, and superose 12 hr 10/30 columns. when these procedures were carried out under strictly anaerobic conditions, approximately 3 mg of this protein could be isolated from ... | 1992 | 1587836 |
| immunological identification and distribution of dissimilatory heme cd1 and nonheme copper nitrite reductases in denitrifying bacteria. | polyclonal antibodies were used to identify heme or copper nitrite reductases in the following groups: 23 taxonomically diverse denitrifiers from culture collections, 100 numerically dominant denitrifiers from geographically diverse environments, and 51 denitrifiers from a culture collection not selected for denitrification. antisera were raised against heme nitrite reductases from pseudomonas aeruginosa and pseudomonas stutzeri and against copper nitrite reductase from achromobacter cycloclaste ... | 1989 | 2624465 |
| glutaredoxin from rabbit bone marrow. purification, characterization, and amino acid sequence determined by tandem mass spectrometry. | a glutaredoxin was purified from rabbit bone marrow, and its amino acid sequence was determined by high performance tandem mass spectrometry. the sequences of peptides generated by digestion with trypsin alone or in combination with thermolysin were determined from their collision-induced dissociation (cid) mass spectra. alignment of these sequences and additional sequence information were obtained from the collision-induced dissociation mass spectra of peptides obtained from digestion of the in ... | 1989 | 2684977 |
| purification, characterization and revised amino acid sequence of a second thioredoxin from corynebacterium nephridii. | a second thioredoxin, distinct from the one reported by meng and hogenkamp in 1981 (j. biol. chem. 256, 9174-9182), has been purified to homogeneity from an escherichia coli strain containing a plasmid encoding a corynebacterium nephridii thioredoxin. thioredoxin genes from c. nephridii were cloned into the plasmid puc13 and transformants were identified by complementation of a thioredoxin negative (trxa-) e. coli strain. the abilities of the transformants to support the growth of several phages ... | 1989 | 2917572 |
| cloning, expression, and nucleotide sequence of a gene encoding a second thioredoxin from corynebacterium nephridii. | a gene encoding thioredoxin in corynebacterium nephridii was cloned in escherichia coli by complementation of a thioredoxin mutant. transformants that appeared to complement were analyzed for the presence of thioredoxin by the coupled assay using methionine sulfoxide reductase. of 18 transformants, four contained high levels of thioredoxin activity. transformants containing plasmids plcn2 and plcn4 were unable to support replication of t7 phage, in spite of their thioredoxin activities, and were ... | 1987 | 3040729 |
| production of nitric oxide and nitrous oxide during denitrification by corynebacterium nephridii. | resting cells of corynebacterium nephridii reduce nitrate, nitrite, and nitric oxide to nitrous oxide under anaerobic conditions. nitrous oxide production from nitrite was optimal from ph 7.0 to 7.4. the stoichiometry of nitrous oxide production from nitrite was 99% of the theoretical-two moles of nitrite was used for each mole of nitrous oxide detected. hydroxylamine increases gas evolution from nitrite but inhibits the reduction of nitric oxide to nitrous oxide. hydroxylamine is converted to n ... | 1970 | 5438050 |
| purification and characterization of thioredoxin from the n2-fixing cyanobacterium anabaena cylindrica. | thioredoxin has been purified to homogeneity from the cyanobacterium anabaena cylindrica. the protein consists of a single polypeptide chain with a relative molecular mass of about 11 680 which has two cysteine residues (residues 31 and 34) in the sequence-cys-gly-pro-cys- and an isoelectric point at ph 4.55. the n-terminal amino acid sequence of 39 residues shows distinct homologies with the sequences of escherichia coli and corynebacterium nephridii thioredoxins. anti-(a. cylindrica thioredoxi ... | 1984 | 6146520 |
| the synthesis and properties of four spin-labeled analogs of adenosylcobalamin. | four spin-labeled analogs of adenosylcobalamin have been synthesized to aid in the detection and identification of radical intermediates in the adenosylcobalamin-dependent enzymatic reactions and to serve as probes of the coenzyme, substrate, and effector binding sites of the protein. three isomers of adenosylcobalamin, in which one of the propionamide side chains (b, d, or e) was hydrolyzed, and adenosylepicobalamin e-carboxylic acid were reacted with 4-amino-2,2,6,6-tetramethylpiperidine-n-oxy ... | 1980 | 6246074 |
| affinity labeling of ribonucleotide reductase by the 2',3'-dialdehyde derivatives of ribonucleotides. | ribonucleotide reductase from corynebacterium nephridii is rapidly inactivated by the 2',3'-dialdehyde derivatives of cdp (dial-cdp) and adp (dial-adp). the analog of cdp causes the progressive inactivation of ribonucleotide reductase activity with ki of 0.26 mm and a maximum inactivation rate of 0.092 min-1 at saturating concentrations of dial-cdp. the modified enzyme remains inactive even after extensive dialysis. the four common nucleoside diphosphates (adp, gdp, cdp, and udp) protect the enz ... | 1983 | 6357087 |
| properties of a thioredoxin purified from rabbit bone marrow which fails to serve as a hydrogen donor for the homologous ribonucleotide reductase. | a thioredoxin has been highly purified from rabbit bone marrow. this thioredoxin is heat-stable, has a molecular weight of approximately 13,000, and contains 4 half-cystines. it is a substrate for the nadph-dependent thioredoxin reductase of rabbit bone marrow, catalyzes the reduction of insulin disulfides by dithiothreitol, and is a hydrogen donor for methionine sulfoxide reductase of yeast. although active as a hydrogen donor for ribonucleotide reductase of lactobacillus leichmannii, this acti ... | 1983 | 6358204 |
| the purification and characterization of an adenosylcobalamin-dependent ribonucleoside diphosphate reductase from corynebacterium nephridii. | a deoxyadenosylcobalamin-dependent ribonucleoside diphosphate reductase has been purified to homogeneity from cell free extracts of corynebacterium nephridii. ion exchange chromatography of th extract on deae-sephadex and deae-bio-gel a, followed by affinity chromatography on dgtp-sepharose, yielded two forms of the reductase. the first reductase, which was weakly bound to the affinity column, was eluted with 0.1 m citrate buffer, ph 6.5, while the second, more tightly bound form required 2 m ur ... | 1980 | 6986368 |
| purification, characterization, and amino acid sequence of thioredoxin from corynebacterium nephridii. | | 1981 | 7021558 |
| 2'-c-methyladenosine and 2'-c-methyluridine 5'-diphosphates are mechanism-based inhibitors of ribonucleoside diphosphate reductase from corynebacterium nephridii. | the interaction of the adenyosylcobalamin-dependent ribonucleoside diphosphate reductase of cornyebacterium nephridii with 2'-c-methyladenosine 5'-diphosphate (2'-meadp) and 2'-c-methyluridine 5'-diphosphate (2'-meudp) has been investigated. the nucleotide analogs are converted to adenine and uracil, respectively, suggesting that they may be mechanism-based inhibitors. in addition, both analogs generate nucleotides with properties expected for the 2'-deoxy-2'-c-methylnucleotides. the nucleoside ... | 1993 | 8218205 |
| mechanism-based inhibition of ribonucleoside diphosphate reductase from corynebacterium nephridii by 2'-c-methyladenosine diphosphate. | the interaction of the adenosylcobalamin-dependent ribonucleoside diphosphate reductase of corynebacterium nephridii with 2'-c-methyladenosine diphosphate (2'-c-methyladp) has been investigated in more detail [ong, s. p., mcfarlan, s. c., & hogenkamp, h. p. c. (1993) biochemistry 32, 11397-11404]. this nucleotide analog partitioned between normal reduction to 2'-deoxy-2'-c-methyladenosine diphosphate and decomposition to adenine, 2-methylene-3(2h)-4-methylfuranone, and presumably pyrophosphate. ... | 1996 | 8605198 |
| identification of a third thioredoxin gene from corynebacterium nephridii. | we identified and sequenced a gene encoding a third thioredoxin (c3) from corynebacterium nephridii. the determined nucleotide sequence encodes a thioredoxin of 145 amino acid residues, which is larger than most thioredoxins found in microbial cells and contains 6 cysteine residues. c. nephridii thioredoxin c3 is able to serve as a subunit of t7 dna polymerase. c. nephridii is the first nonphotosynthetic procaryotic organism known to carry three different thioredoxins. | 1996 | 8652661 |
| denitrification by corynebacterium nephridii. | hart, lewis t. (louisiana state university, baton rouge), a. d. larson, and c. s. mccleskey. denitrification by cornyebacterium nephridii. j. bacteriol. 89:1104-1108. 1965.-corynebacterium nephridii was found to reduce nitrate (contrary to the original description) at a rapid rate. in the conventional 0.1% nitrate broth, neither nitrite nor nitrate was detected after 24 hr. there was no assimilation of nitrate nitrogen, and the final product of nitrate reduction was nitrous oxide. manometric stu ... | 1965 | 14276103 |
| criteria and methodology for identifying respiratory denitrifiers. | respiratory denitrification is not always adequately established when bacteria are characterized. we have tested a simple method that allows one to evaluate whether the two necessary criteria to claim denitrification have been met, namely, that n(inf2) or n(inf2)o is produced from nitrate or nitrite and that this reduction is coupled to a growth yield increase. microorganisms were cultured in sealed tubes under a helium headspace and in the presence of 0, 2, 4, 7, and 10 mm nitrate or nitrite. a ... | 1995 | 16534960 |
| pcr cloning of a protein-coding part of the thioredoxin gene fromstreptomyces aureofaciens. | the method of two-stage half-specific amplification was described and successfully used in the isolation of the protein-coding part of the thioredoxin gene from streptomyces aureofaciens bmk. the efficiency of a new pcr modification for the specific amplification of the target dna fragments (genes) with unknown sequences is compared with the used half-specific pcr. the determined target sequence demonstrates the highest homology with the thioredoxin genes from corynebacterium nephridii c-1 and a ... | 1994 | 24190746 |