Coverart for item
The Resource Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book)

Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book)

Label
Metal-carbon bonds in enzymes and cofactors
Title
Metal-carbon bonds in enzymes and cofactors
Statement of responsibility
edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel
Contributor
Subject
Language
eng
Summary
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
Member of
Cataloging source
MiAaPQ
Dewey number
572.7
Illustrations
illustrations
Index
index present
LC call number
QP601.7
LC item number
.M47 2009
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
  • Sigel, Astrid
  • Sigel, Helmut
  • Sigel, Roland K. O
Series statement
Metal ions in life sciences
Series volume
6
http://library.link/vocab/subjectName
  • Metalloenzymes
  • Coenzymes
  • Organometallic compounds
  • Vitamin B12
Label
Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book)
Instantiates
Publication
Bibliography note
Includes bibliographical references and indexes
Carrier category
online resource
Carrier MARC source
rdacarrier
Color
multicolored
Content category
text
Content type MARC source
rdacontent
Contents
Organometallic chemistry of B12 coenzymes -- Cobalamin- and corrinoid-dependent enzymes -- Nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase -- Nickel-carbon bonds in acetyl-coenzyme a synthases/carbon monoxide dehydrogenases -- Structure and function of [NiFe]-hydro-genases -- Carbon monoxide and cyanide ligands in the active site of [FeFe]-hydrogenases -- Carbon monoxide as intrinsic ligand to iron in the active site of [Fe]-hydrogenase -- Dual role of heme as cofactor and substrate in the biosynthesis of carbon monoxide -- Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site -- Interaction of cyanide with enzymes containing vanadium, manganese, non-heme iron, and zinc -- Reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds
Control code
EBC5024742
Dimensions
unknown
Extent
1 online resource (532 pages)
Form of item
online
Isbn
9783110436587
Media category
computer
Media MARC source
rdamedia
Note
Electronic reproduction. Ann Arbor, MI : ProQuest, 2018. Available via World Wide Web. Access may be limited to ProQuest affiliated libraries.
Other physical details
illustrations (some color).
Sound
unknown sound
Specific material designation
remote
Label
Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book)
Publication
Bibliography note
Includes bibliographical references and indexes
Carrier category
online resource
Carrier MARC source
rdacarrier
Color
multicolored
Content category
text
Content type MARC source
rdacontent
Contents
Organometallic chemistry of B12 coenzymes -- Cobalamin- and corrinoid-dependent enzymes -- Nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase -- Nickel-carbon bonds in acetyl-coenzyme a synthases/carbon monoxide dehydrogenases -- Structure and function of [NiFe]-hydro-genases -- Carbon monoxide and cyanide ligands in the active site of [FeFe]-hydrogenases -- Carbon monoxide as intrinsic ligand to iron in the active site of [Fe]-hydrogenase -- Dual role of heme as cofactor and substrate in the biosynthesis of carbon monoxide -- Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site -- Interaction of cyanide with enzymes containing vanadium, manganese, non-heme iron, and zinc -- Reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds
Control code
EBC5024742
Dimensions
unknown
Extent
1 online resource (532 pages)
Form of item
online
Isbn
9783110436587
Media category
computer
Media MARC source
rdamedia
Note
Electronic reproduction. Ann Arbor, MI : ProQuest, 2018. Available via World Wide Web. Access may be limited to ProQuest affiliated libraries.
Other physical details
illustrations (some color).
Sound
unknown sound
Specific material designation
remote

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