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Metal-Carbon Bonds in Enzymes and Cofactors de Astrid Sigel

Metal-Carbon Bonds in Enzymes and Cofactors: Metal Ions in Life Sciences, cartea 6

Editat de Astrid Sigel, Helmut Sigel, Roland K. O. Sigel
en Limba Engleză Hardback – 31 dec 2008
The occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, is only recently appreciated. 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. MILS-6, written by 20 experts, summarizes the most recent insights into this fascinating topic.
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Specificații

ISBN-13: 9783110442793
ISBN-10: 3110442795
Pagini: 530
Ilustrații: 50 schw.-w. u. 30 farb. Abb., 50 schw.-w. Tab.
Dimensiuni: 155 x 235 x 34 mm
Greutate: 0.92 kg
Editura: De Gruyter
Colecția De Gruyter
Seria Metal Ions in Life Sciences

Locul publicării:Berlin/Boston

Notă biografică

Helmut und Astrid Sigel, University of Basel, Switzerland. Roland K. O. Sigel, University of Zürich, Switzerland.

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From the Content:

• 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]-Hydrogenases • 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 • The 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 • The Reaction Mechanism of the Molybdenum Hydroxylase Xanthine Oxidoreductase: Evidence Against the Formation of Intermediates Having Metal-Carbon Bonds • Computational Studies of Biooganometalllic Enzymes and Cofactors

Descriere

Descriere de la o altă ediție sau format:
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. Metal-Carbon Bonds in Enzymes and Cofactors, Volume 6, written by 17 experts, summarizes the most recent insights into this fascinating topic.

Recenzii

Mainly coenzyme B12
Metal-carbon bonds in enzymes and cofactors
Series: Metal Ions in Life Sciences , Vol. 6
A. Sigel, H. Sigel and R.K.O Sigel (Eds)
RSC Publishing, Cambridge, UK, 2009, 544pp. (HB) ISBN 9781847559159
 
Reviewed by Kevin Waldron
This, the latest in the excellent Metal ions in life sciences series, focuses on biological molecules that contain a metal-carbon bond. The most familiar molecule of this class is coenzyme B12, whose structural determination in 1956 by Dorothy Hodgkin confirmed the presence of a cobalt-carbon bond. This was the first such example, arguably marking the beginning of the field of bio-organometallic chemistry and contributing to Hodgkin's achievements recognized with the Nobel prize for chemistry in 1964.
B12 remains well studied today, partly due to the fact that its biosynthesis is achieved only by microorganisms and that dietary deficiency results in pernicious anemia in humans. Indeed, such research is still revealing some molecular surprises, such as the relatively recent discovery of the B12-sensing riboswitch that regulates gene expression in response to available B12 concentration. 
After dealing with the organometallic chemistry and enzymatic utilization of B12 in chapters one and two, this book concentrates primarily on the interaction of CO and CN- with metal ions. These latter ligands are usually regarded as solely toxic molecules, but perhaps surprisingly are physiological ligands to Fe and Ni ions in the active sites of hydrogenase enzymes, whereas CO is produced by the activities of metal-dependent enzymes such as haem oxygenase and acetyl coenzyme A synthase. They are also useful as spectroscopic tools to interrogate a range of metal binding sites for chemical and structural information in vitro, covered in later chapters.
As with all books of this series, the combination of cost and subject matter means that this book is predominantly intended as a primary resource for researchers working in the field, but will surely also prove useful for undergraduates as a gateway to the subject with its extensive reference list.
Chemistry World, 2009, 6(11), p. 65

Caracteristici

The books appearing in the series uniquely link coordination chemistry and biochemistry in their widest sense