GLORIA

GEOMAR Library Ocean Research Information Access

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Online Resource
    Online Resource
    Metal-carbon bonds in enzymes and cofactors : Volume 6 (2009)
    Cambridge : Royal Society of Chemistry
    Details Availability
    Keywords: Coenzymes ; Coenzymes chemistry ; Metalloenzymes ; Multienzyme Complexes chemistry ; Organometallic Compounds chemistry ; Organometallic compounds ; Oxidoreductases chemistry ; Vitamin B 12 chemistry ; Vitamin B12 ; Metallorganische Verbindungen ; Enzym ; Cofaktor
    Description / Table of Contents: This book covers the occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, The occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, is only recently recognized. Of course, the historical examples are the B12 coenzymes containing cobalt-carbon bonds, but now such bonds are also known for nickel, iron, copper, and other transition metal ions. There is no other comparable book; MILS-6, written by 17 experts, summarizes the most recent insights into this fascinating topic
    Type of Medium: Online Resource
    Pages: Online-Ressource (488 p)
    Edition: RSC eBook Collection 1968-2009
    ISBN: 1847559336 , 9781847559333
    Series Statement: Metal ions in life sciences 6
    URL: http://www.rsc.org/Publishing/eBooks/2009/9781847559159.asp
    URL: https://doi.org/10.1039/9781847559333
    URL: http://www.gbv.de/dms/bowker/toc/9781847559333.pdf
    RVK:
    VH 9750
    Language: English
    Note: Ebook , Chapter 1: ORGANOMETALLIC CHEMISTRY OF B12 COENZYMES-- Chapter 2: COBALAMIN- AND CORRINOID-DEPENDENT ENZYMES-- Chapter 3: NICKEL-ALKYL BOND FORMATION IN THE ACTIVE SITE OF METHYL-COENZYME M REDUCTASE-- Chapter 4: NICKEL-CARBON BONDS IN ACETYL-COENZYME A SYNTHASES/CARBON MONOXIDE DEHYDROGENASES-- Chapter 5: STRUCTURE AND FUNCTION OF [NiFe]-HYDROGENASES-- Chapter 6: CARBON MONOXIDE AND CYANIDE LIGANDS IN THE ACTIVE SITE OF [FeFe]-HYDROGENASES-- Chapter 7: CARBON MONOXIDE AS INTRINSIC LIGAND TO IRON IN THE ACTIVE SITE OF [Fe]-HYDROGENASE-- Chapter 8: THE DUAL ROLE OF HEME AS COFACTOR AND SUBSTRATE IN THE BIOSYNTHESIS OF CARBON MONOXIDE-- Chapter 9: COPPER-CARBON BONDS IN MECHANISTIC AND STRUCTURAL PROBING OF PROTEINS AS WELL AS IN SITUATIONS WHERE COPPER IS A CATALYTIC OR RECEPTOR SITE-- Chapter 10: INTERACTION OF CYANIDE WITH ENZYMES CONTAINING VANADIUM, MANGANESE, NON-HEME IRON, AND ZINC-- Chapter 11: THE REACTION MECHANISM OF THE MOLYBDENUM HYDROXYLASE XANTHINE OXIDOREDUCTASE: EVIDENCE AGAINST THE FORMATION OF INTERMEDIATES HAVING METAL-CARBON BONDS-- Chapter 12: COMPUTATIONAL STUDIES OF BIOORGANOMETALLIC ENZYMES AND COFACTORS.
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    GEOMAR CATALOGUE
    Link to Library Catalog
    get availability status
  • 2
    Electronic Resource
    Electronic Resource
    The DNA binding protein Tfx from Methanobacterium thermoautotrophicum: structure, DNA binding properties and transcriptional regulation (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 31 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In Methanobacterium thermoautotrophicum, the fmdECB operon encoding the molybdenum formylmethanofuran dehydrogenase is directly preceded by an open reading frame tfx predicted to encode a DNA binding protein. The 16.1 kDa protein has an N-terminal basic domain with a helix–turn–helix motif for DNA binding and a C-terminal acidic domain possibly for transcriptional activation. We report here on the DNA binding properties of the Tfx protein heterologously overproduced in Escherichia coli. Tfx was found to bind specifically to a DNA sequence downstream of the promoter of the fmdECB operon, as shown by electrophoretic mobility shift assays and DNase I footprint analysis. Northern blot hybridizations revealed that transcription of tfx is repressed during the growth of M. thermoautotrophicum in the presence of tungstate. Based on its structure and properties, the DNA binding protein Tfx is proposed to be a transcriptional regulator composed of a basic DNA binding domain and an acidic activation domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01204.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri (1997)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 23 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The genome of Methanopyrus kandleri was found to harbour a gene, fwuB, predicted to encode the catalytic subunit of a tungsten formylmethanofuran dehydrogenase with an active site selenocysteine, and a second gene, fwcB, encoding a tungsten formylmethanofuran dehydrogenase with an active site cysteine. Northern blot and primer-extension analysis revealed that both genes were differentially transcribed. During growth of the methanogen on medium supplemented with selenium only fwuB was transcribed, whereas transcription of both fwuB and fwcB was observed on selenium-deprived medium. Growth of M. kandleri was stimulated by tungstate and selenite but not by molybdate. The findings indicate that the hyperthermophilic archaeon contains two tungsten isoenzymes of formylmethanofuran dehydrogenase, one of which is a novel selenium enzyme. They also indicate that the hyperthermophilic methanogen probably does not contain a molybdenum formylmethanofuran dehydrogenase which appears to be present only in thermophilic and mesophilic methanogens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.2931653.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...