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)
Resource Information
The item Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book) represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in Sydney Jones Library, University of Liverpool.This item is available to borrow from 1 library branch.
Resource Information
The item Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book) represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in Sydney Jones Library, University of Liverpool.
This item is available to borrow from 1 library branch.
- 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
- Language
- eng
- Extent
- 1 online resource (532 pages)
- 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
- Isbn
- 9783110436587
- 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
- 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
- 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)
- 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)
- 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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<div class="citation" vocab="http://schema.org/"><i class="fa fa-external-link-square fa-fw"></i> Data from <span resource="http://link.liverpool.ac.uk/portal/Metal-carbon-bonds-in-enzymes-and-cofactors/aTW9PBn4kzY/" typeof="Book http://bibfra.me/vocab/lite/Item"><span property="name http://bibfra.me/vocab/lite/label"><a href="http://link.liverpool.ac.uk/portal/Metal-carbon-bonds-in-enzymes-and-cofactors/aTW9PBn4kzY/">Metal-carbon bonds in enzymes and cofactors, edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel, (electronic book)</a></span> - <span property="potentialAction" typeOf="OrganizeAction"><span property="agent" typeof="LibrarySystem http://library.link/vocab/LibrarySystem" resource="http://link.liverpool.ac.uk/"><span property="name http://bibfra.me/vocab/lite/label"><a property="url" href="http://link.liverpool.ac.uk/">Sydney Jones Library, University of Liverpool</a></span></span></span></span></div>
