GLORIA

GEOMAR Library Ocean Research Information Access

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
    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
    RVK:
    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 ...
  • 2
    ISSN: 1432-072X
    Keywords: Archaea ; Methanogens ; Trimethylamine metabolism ; Methyltransferases ; Methyl ; coenzyme M ; Methylcobalamin ; Corrinoids ; Vitamin B12
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanosarcina barkeri was recently shown to contain two cytoplasmic isoenzymes of methylcobalamin: coenzyme M methyltransferase (methyltransferase 2). Isoenzyme I predominated in methanol-grown cells and isoenzyme II in acetate-grown cells. It was therefore suggested that isoenzyme I functions in methanogenesis from methanol and isoenzyme II in methanogenesis from acetate. We report here that cells of M. barkeri grown on trimethylamine, H2/CO2, or acetate contain mainly isoenzyme II. These cells were found to have in common that they can catalyze the formation of methane from trimethylamine and H2, whereas only acetate-grown cells can mediate the formation of methane from acetate. Methanol-grown cells, which contained only low concentrations of isoenzyme II, were unable to mediate the formation of methane from both trimethylamine and acetate. These and other results suggest that isoenzyme II (i) is employed for methane formation from trimethylamine rather than from acetate, (ii) is constitutively expressed rather than trimethylamine-induced, and (iii) is repressed by methanol. The constitutive expression of isoenzyme II in acetate-grown M. barkeri can explain its presence in these cells. The N-terminal amino acid sequences of isoenzyme I and isoenzyme II were analyzed and found to be only 55% similar.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...