Metal-Carbon Bonds in Enzymes and Cofactors.
نویسنده
چکیده
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.
منابع مشابه
Preface to Volume 6 Metal-Carbon Bonds in Enzymes and Cofactors
This is the 6th volume within the MILS series; together with the 44 volumes published in our former series Metal Ions in Biological Systems this sums up to in total 50 books. This event is celebrated with a comprehensive Author Index, given at the end of this book. It encompasses the names of all colleagues who contributed to these 44 MIBS and 6 MILS volumes. All these authors deserve our speci...
متن کاملOrganometallic chemistry of b(12) coenzymes.
When coenzyme B(12) was identified as organometallic derivative of vitamin B(12), metal-carbon bonds were revealed to be relevant in life processes. Vitamin B(12), the "antipernicious anaemia factor" required for human health, was isolated earlier as a crystallizable cyano-Co(III)-complex. B(12) cofactors and other cobalt corrinoids play important roles not only in humans, but in the metabolism...
متن کاملRadical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.
Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. The FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has C...
متن کاملThe biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.
Sulfur atoms are present as thiol and thioether functional groups in amino acids, coenzymes, cofactors, and various products of secondary metabolic pathways. The biosynthetic pathways for several sulfur-containing biomolecules require the substitution of sulfur for hydrogen at unreactive aliphatic or electron-rich aromatic carbon atoms. Examples discussed in this review include biotin, lipoic a...
متن کاملDynamic 1H NMR Study Around the Carbon–Carbon Double Bonds and Carbon–Carbon Single Bonds in a Particular Phosphorous Ylide and 2,5-Dihydro-5,5-Diaryl-2-Thio-1H-Imidazoles
Stable crystalline phosphorus ylides are obtained in excellent yields from the 1:1:1 addition reactionbetween hydantoins or thiohydantoins and dialkyl acetylenedicarboxylates in the presence oftriphenylphosphine. These phosphoranes undergo smooth intramolecular Wittig reaction followedby an electrocyclic ring opening to produce dialkyl (E)-2-(2,5-dihydro-5,5-diaryl-2-thioxo-1H-imidazol-4-yl)fum...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Coordination chemistry reviews
دوره 254 17-18 شماره
صفحات -
تاریخ انتشار 2010