By Astrid Sigel, Helmut Sigel, Roland K O Sigel, Bernhard Kraeutler
ISBN-10: 1847559158
ISBN-13: 9781847559159
The prevalence of a wide selection of metal-carbon bonds in dwelling organisms, starting from micro organism to people, is just lately well-known. in fact, the old examples are the B12 coenzymes containing cobalt-carbon bonds, yet now such bonds also are recognized for nickel, iron, copper, and different transition steel ions.
There isn't any different similar booklet. Metal-Carbon Bonds in Enzymes and Cofactors, Volume 6, written via 17 specialists, summarizes the newest insights into this interesting topic.
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Additional info for Metal-Carbon Bonds in Enzymes and Cofactors
Example text
Perhaps B12 coenzymes are Nature’s physiologically most relevant organometallic cofactors [9–12]. Organometallic B12 derivatives engage in protein-activated reactions in unique B12-dependent enzymes. In these, B12 cofactors (co)catalyze exceptional enzymatic reactions [18–23] that directly depend upon the reactivity of the cobalt-carbon bond [11,12,22]. Since the surprising identification of coenzyme B12 as an organometallic compound, corrinoid cofactors have thus played central roles in the discovery and better understanding of biological organometallic processes [24–28].
However, in the ‘‘neo’’ corrinoid 10, the configuration at the corrin ring C was inverted, apparently reducing the steric hindrance due to a propionate side chain, and making the dimer formation possible [56]. The crystal structure of heptamethyl-cob(II)yrinate (cob(II)ester (as the perchlorate complex 11) gave the first detailed insights into the structure of a paramagnetic Co(II)-corrin [57]. 31 A˚) [57]. The coordination of the axial ligand at the sterically less hindered ‘‘upper’’ b-face is in contrast with the preference seen in the ‘‘complete’’ cob(II)alamin (6, B12r) [58,59] (see below).
Modern, 2D-ESR techniques have also allowed the detection of external ligands to ‘‘incomplete’’ Co(II)-corrins in (frozen) solution, such as Co(II)cobester (11) [117], and in the protonated, base-off-form of cob(II)alamin (6-H1) [118]. The application of modern methods of absorbance spectroscopy, combined with theory-based interpretation of the data has also opened a new look at Met. Ions Life Sci. , [119,120] and Chapter 12 of this book). 3. The ‘‘Base-On/Base-Off’’ Constitutional Switch of ‘‘Complete’’ Corrinoids The typical functional B12 cofactors are ‘‘complete’’ corrinoids, and are unique conjugates of natural cobyrinates with unusual a-nucleotide function [6,11,12].