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  1. Article: Deoxyribonucleotides: the unusual chemistry and biochemistry of DNA precursors.

    Follmann, Hartmut

    Chemical Society reviews

    2004  Volume 33, Issue 4, Page(s) 225–233

    Abstract: Deoxyribonucleotides, monomers of macromolecular DNA and the chemical matter of genes, have received surprisingly little attention among chemists and molecular biologists alike, although their origin, properties, and mechanism of enzyme-catalyzed ... ...

    Abstract Deoxyribonucleotides, monomers of macromolecular DNA and the chemical matter of genes, have received surprisingly little attention among chemists and molecular biologists alike, although their origin, properties, and mechanism of enzyme-catalyzed formation bear unique chemical traits which are the basis of DNA replication. Apart from providing insights in bioorganic free radical chemistry, present interest in deoxyribonucleotides stems from the expected demand of hundreds of kilograms per year for DNA chips and antisense constructs used in gene therapy, difficult to produce by conventional methods. A novel approach towards deoxyribonucleotide, and hence DNA formation in a putative primordial 'RNA world' has also recently emerged.
    MeSH term(s) Animals ; Biomimetics ; Catalysis ; DNA/chemistry ; DNA/isolation & purification ; DNA Replication ; DNA, Antisense/chemical synthesis ; Deoxyribonucleotides/biosynthesis ; Deoxyribonucleotides/chemistry ; Deoxyribose/chemistry ; Evolution, Molecular ; Genetic Therapy ; Nucleic Acid Precursors/chemistry ; Nucleic Acid Precursors/metabolism ; Oligonucleotide Array Sequence Analysis ; Oxidation-Reduction ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/classification ; Ribonucleotide Reductases/metabolism
    Chemical Substances DNA, Antisense ; Deoxyribonucleotides ; Nucleic Acid Precursors ; Deoxyribose (533-67-5) ; DNA (9007-49-2) ; Ribonucleotide Reductases (EC 1.17.4.-)
    Language English
    Publishing date 2004-05-10
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/a907361b
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  2. Article: Irregularities in the Circular Dichroism of Oligoribonucleotides

    Zacharias, Wolfgang / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 37, no. 7-8

    2014  

    Abstract: Marked anomalies, previously unresolved, exist in the CD spectra of oligoadenylates and oligouridylates at the pentamer or tetramer stage, indicating that these molecules differ in conformation from the preceding and the following member of the series. ... ...

    Abstract Marked anomalies, previously unresolved, exist in the CD spectra of oligoadenylates and oligouridylates at the pentamer or tetramer stage, indicating that these molecules differ in conformation from the preceding and the following member of the series. The CD of oligoadenylates retains a positive Cotton effect even at 80 °C. Caution must be exerted when predicting oligonucleotide structures from CD spectra.
    Keywords circular dichroism spectroscopy ; oligoribonucleotides ; prediction
    Language English
    Dates of publication 2014-0602
    Size p. 727-730.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1982-7-827
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  3. Article: Notes: Formation of Large Thioredoxin f Accompanies Chloroplast Development in Scenedesmus obliquus

    Langlotz, Petra / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 42, no. 11-12

    2014  

    Abstract: Chloroplast-free mutant cells C-2A′ of the green algae Scenedesmus obliquus lack thioredoxin f, which functions in the light activation of chloroplast enzymes, but do con­tain the regular thioredoxins I and II. When dark-grown algae are transferred to ...

    Abstract Chloroplast-free mutant cells C-2A′ of the green algae Scenedesmus obliquus lack thioredoxin f, which functions in the light activation of chloroplast enzymes, but do con­tain the regular thioredoxins I and II. When dark-grown algae are transferred to light, thioredoxin f activity appears rapidly and increases in parallel with photosynthetic ac­tivities: however it precedes chlorophyll biosynthesis. The formation of thioredoxin f is inhibited by cydoheximide indicating that it occurs on the cytoplasmic ribosomes, in accord with the lack of thioredoxin genes on the chloroplast genomes.
    Keywords algae ; biosynthesis ; chlorophyll ; chloroplast genome ; chloroplast thioredoxins ; chloroplasts ; genes ; mutants ; photosynthesis ; ribosomes ; Scenedesmus obliquus
    Language English
    Dates of publication 2014-0602
    Size p. 1364-1366.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1987-11-1241
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  4. Article: Characterization of Two Thioredoxins in Pig Heart Including a New Mitochondrial Protein

    Bodenstein, Johanna / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 46, no. 3-4

    2014  

    Abstract: Heart tissue contains two different thioredoxins. One is a specific mitochondrial protein and is best prepared from pre-isolated, intact heart mitochondria (mt-thioredoxin) whereas mitochondria-depleted tissue homogenates contain the major cellular ... ...

    Abstract Heart tissue contains two different thioredoxins. One is a specific mitochondrial protein and is best prepared from pre-isolated, intact heart mitochondria (mt-thioredoxin) whereas mitochondria-depleted tissue homogenates contain the major cellular thioredoxin of cytoplasmic origin (c-thioredoxin). Both heat-stable proteins are clearly differentiated chrom atographically. They exhibit slightly different molecular weights (12300 vs. 12000) and isoelectric points (4.7 vs. 4.8) but differ remarkably in their cysteine content: mt-Thioredoxin has two cysteine residues like the bacterial proteins, and c-thioredoxin possesses six cysteines. Heart extracts were also show n to contain a NADPH-specific thioredoxin reductase of the known mammalian type. A specific function or target enzyme of mt-thioredoxin has not as yet been established.
    Keywords bacterial proteins ; cysteine ; heart ; heat stability ; isoelectric point ; mitochondria ; molecular weight ; swine ; thioredoxins
    Language English
    Dates of publication 2014-0602
    Size p. 270-279.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1991-3-418
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  5. Article: Deoxyribonucleotide Synthesis in Phycovirus-Infected Green Algae. A New Virus-Induced Ribonucleotide Reductase

    Bornemann, Claus / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 48, no. 1-2

    2014  

    Abstract: Infection of Chlorella-like green algae with freshwater phycoviruses is associated with a large and rapid demand for DNA precursors which cannot be met by the algal deoxyribonucleotide-synthesizing enzymes. We have demonstrated in these cells an up to ... ...

    Abstract Infection of Chlorella-like green algae with freshwater phycoviruses is associated with a large and rapid demand for DNA precursors which cannot be met by the algal deoxyribonucleotide-synthesizing enzymes. We have demonstrated in these cells an up to ten-fold increase of the key enzyme, ribonucleotide reductase, 1-2 h post infection. The enzyme activity has been partially enriched from cell extracts. In vitro, it differs from that of uninfected algae in three characteristic parameters, viz. eight-fold higher resistance to millimolar hydroxyurea concentrations, much higher optimum concentration of an allosteric effector nucleotide, thymidine triphosphate, and an unusually low temperature optimum at 20 °C. We conclude that the large DNA phycoviruses, like Herpes and pox viruses, code for their own specific ribonucleotide reductase.
    Keywords algae ; Chlorophyta ; DNA ; enzyme activity ; freshwater ; hydroxyurea ; ribonucleotide reductase ; temperature ; thymidine ; viruses
    Language English
    Dates of publication 2014-0602
    Size p. 113-118.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1993-1-222
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  6. Article: Deoxyribonucleotide Biosynthesis in Green Algae. S Phase-Specific Thymidylate Kinase and Unspecific Nucleoside Diphosphate Kinase in Scenedesmus obliquus

    Klein, Beate / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 43, no. 5-6

    2014  

    Abstract: NDP kinase and thymidylate kinase are essential for DNA precursor formation in that they phosphorylate the products of de novo deoxyribonucleotide biosynthesis, deoxyribonucleoside 5′-diphosphates and thymidine 5′-monophosphate to the corresponding ... ...

    Abstract NDP kinase and thymidylate kinase are essential for DNA precursor formation in that they phosphorylate the products of de novo deoxyribonucleotide biosynthesis, deoxyribonucleoside 5′-diphosphates and thymidine 5′-monophosphate to the corresponding triphosphates which then serve as DNA polymerase substrates. The two enzymes have been measured in synchronous cultures of the green algae, S. obliquus. Thymidylate kinase exhibits an activity peak at the 11 -12th hour of the 24-hour cell cycle, coinciding with DNA synthesis. Enzyme activity is markedly stimulated in presence of fluorodeoxyuridine in the culture medium. This behaviour of dTMP kinase is very similar to that of three other S phase-specific peak enzymes previously analyzed in synchronous algae, viz. ribonucleotide reductase, thymidylate synthase, and dihydrofolate reductase. In contrast, NDP kinase exhibits high and constant activity through the entire cell cycle. The two kinases have been isolated from cell-free extracts, and separated from each other by chromatography on Blue Sepharose. The peak enzyme, dTMP kinase, has been purified to near homogeneity and its catalytic properties are described; the molecular weight is 56,000. NDP kinase activity is separable into two enzyme fractions, both of molecular weight 100,000 (or higher), which are unspecific with respect to ribonucleotide and deoxyribonucleotide substrates. Characterization and purification of the whole series of deoxyribonucleotide-synthesizing enzymes from one organism provides a basis for in vitro experiments towards reconstitution of an S phase-specific DNA precursor/DNA replication multienzyme aggregate.
    Keywords agarose ; algae ; biosynthesis ; cell cycle ; chromatography ; culture media ; dihydrofolate reductase ; DNA ; DNA replication ; DNA-directed DNA polymerase ; enzyme activity ; in vitro studies ; molecular weight ; nucleoside-diphosphate kinase ; ribonucleotide reductase ; Scenedesmus obliquus ; thymidine ; thymidylate synthase
    Language English
    Dates of publication 2014-0602
    Size p. 377-385.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1988-5-610
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  7. Article: A Study of the Substrate and Inhibitor Specificities of AMP Aminohydrolase, 5′-Nucleotidase, and Adenylate Kinase with Adenosine Carboxylates of Variable Chain Length

    Meyer, Wilfried / Hartmut Follmann

    Zeitschrift für Naturforschung C. 2014 June 2, v. 35, no. 3-4

    2014  

    Abstract: A series of AMP analogs in which a terminal carboxylate residue, linked to C4′ of the ribose moiety of adenosine by zero, one, or two methylene groups (1, 2 ,3) or by the unsaturated ethylidene link (4) replaces the phosphate anion, is tested for ... ...

    Abstract A series of AMP analogs in which a terminal carboxylate residue, linked to C4′ of the ribose moiety of adenosine by zero, one, or two methylene groups (1, 2 ,3) or by the unsaturated ethylidene link (4) replaces the phosphate anion, is tested for activity as substrates or effectors of three enzymes known to interact with AMP with a different degree of specificity. 2 - 4 are substrates of AMP aminohydrolase, 3 and 4 are competitive inhibitors of adenylate kinase, and all acids produce competitive inhibition of the least specific enzyme, 5′-nucleotidase. These activities can be cor­ related with the intramolecular flexibility of anionic substituent and adenine base which in turn is expressed in typical shifts of the proton magnetic resonance signal of purine H-8. The uronic acid 1, having a rigid molecular conformation, is inactive towards two AMP-dependent enzymes and little active with the third, indicating that this type of compound is not suitable as a nucleotide an­ tagonist whereas nucleoside carboxylates of type 2 and 3 have a higher potential as effectors of nucleotide metabolism.
    Keywords acids ; adenine ; adenosine ; adenosine monophosphate ; adenylate kinase ; AMP deaminase ; metabolism ; molecular conformation ; nuclear magnetic resonance spectroscopy ; phosphates ; ribose ; uronic acids
    Language English
    Dates of publication 2014-0602
    Size p. 273-278.
    Publishing place Verlag der Zeitschrift für Naturforschung
    Document type Article
    ZDB-ID 124636-7
    ISSN 1865-7125 ; 0341-0382 ; 0341-0471 ; 0939-5075
    ISSN (online) 1865-7125
    ISSN 0341-0382 ; 0341-0471 ; 0939-5075
    DOI 10.1515/znc-1980-3-416
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  8. Article: Deoxyribonucleotides: the unusual chemistry and biochemistry of DNA precursors

    Follmann, Hartmut

    Chemical Society reviews. 2004 Apr. 22, v. 33, no. 4

    2004  

    Abstract: Deoxyribonucleotides, monomers of macromolecular DNA and the chemical matter of genes, have received surprisingly little attention among chemists and molecular biologists alike, although their origin, properties, and mechanism of enzyme-catalyzed ... ...

    Abstract Deoxyribonucleotides, monomers of macromolecular DNA and the chemical matter of genes, have received surprisingly little attention among chemists and molecular biologists alike, although their origin, properties, and mechanism of enzyme-catalyzed formation bear unique chemical traits which are the basis of DNA replication. Apart from providing insights in bioorganic free radical chemistry, present interest in deoxyribonucleotides stems from the expected demand of hundreds of kilograms per year for DNA chips and antisense constructs used in gene therapy, difficult to produce by conventional methods. A novel approach towards deoxyribonucleotide, and hence DNA formation in a putative primordial ‘RNA world’ has also recently emerged.
    Keywords DNA ; DNA microarrays ; DNA replication ; catalytic activity ; free radicals ; gene therapy ; genes
    Language English
    Dates of publication 2004-0422
    Size p. 225-233.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472875-8
    ISSN 1460-4744 ; 0306-0012
    ISSN (online) 1460-4744
    ISSN 0306-0012
    DOI 10.1039/a907361b
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  9. Article ; Online: Darwin's warm little pond revisited: from molecules to the origin of life.

    Follmann, Hartmut / Brownson, Carol

    Die Naturwissenschaften

    2009  Volume 96, Issue 11, Page(s) 1265–1292

    Abstract: All known cosmic and geological conditions and laws of chemistry and thermodynamics allow that complex organic matter could have formed spontaneously on pristine planet Earth about 4,000 mya. Simple gasses and minerals on the surface and in oceans of the ...

    Abstract All known cosmic and geological conditions and laws of chemistry and thermodynamics allow that complex organic matter could have formed spontaneously on pristine planet Earth about 4,000 mya. Simple gasses and minerals on the surface and in oceans of the early Earth reacted and were eventually organized in supramolecular aggregates and enveloped cells that evolved into primitive forms of life. Chemical evolution, which preceded all species of extant organisms, is a fact. In this review, we have concentrated on experimental and theoretical research published over the last two decades, which has added a wealth of new details and helped to close gaps in our previous understanding of this multifaceted field. Recent exciting progress in the molecular and genetic analyses of existing life, in particular microorganisms of ancient origin, even supports the possibility that a cellular, self-reproducing common ancestor might be assembled and resurrected in anaerobic cultures at some time in the future. Charles Darwin did not, and indeed, could not, address and specify the earliest phases of life which preceded the Origin of Species. However, in a famous letter, he sketched "a warm little pond with all sorts of... (chemicals, in which) ...a protein was chemically formed." We try to trace the impact of his charming clear-sighted metaphor up to the present time.
    MeSH term(s) Animals ; Biological Evolution ; Biology/history ; Carbohydrates/chemistry ; Chemistry/history ; Earth, Planet ; Genetic Variation ; History, 19th Century ; Mutation ; Nucleic Acids/chemistry ; Origin of Life ; Poaceae/physiology ; Species Specificity ; Thermodynamics
    Chemical Substances Carbohydrates ; Nucleic Acids
    Language English
    Publishing date 2009-09-17
    Publishing country Germany
    Document type Biography ; Historical Article ; Journal Article ; Review
    ZDB-ID 123257-5
    ISSN 1432-1904 ; 0028-1042
    ISSN (online) 1432-1904
    ISSN 0028-1042
    DOI 10.1007/s00114-009-0602-1
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  10. Book: Biochemie

    Follmann, Hartmut

    Grundlagen und Experimente

    (Teubner-Studienbücher)

    2001  

    Author's details Hartmut Follmann
    Series title Teubner-Studienbücher
    Keywords Biochemie
    Language German
    Size 246 S, graph. Darst, 21 cm
    Edition 1. Aufl
    Publisher Teubner
    Publishing place Stuttgart u.a.
    Document type Book
    Note Literaturverz. S. 238 - 239
    ISBN 3519003333 ; 9783519003335
    Database Former special subject collection: coastal and deep sea fishing

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