scholarly journals Conversion of Vitamin B12 to Coenzyme B12 in Cell-free Extracts of Clostridium tetanomorphum

1961 ◽  
Vol 236 (7) ◽  
pp. PC40-PC42 ◽  
Author(s):  
Herbert Weissbach ◽  
Betty Redfield ◽  
Alan Peterkofsky
Blood ◽  
1973 ◽  
Vol 41 (4) ◽  
pp. 549-557 ◽  
Author(s):  
Lawrence Kass

Abstract Histone biosynthesis was investigated in proerythroblasts and megaloblasts obtained from patients with untreated pernicious anemia. Radioautography, using tritium-labeled L-arginine, L-lysine, and L-trytophane, acrylamide gel electrophoresis of histone fractions, acrylamide gel radioautography, uptake of radioisotopes into lysine-rich and arginine-rich histone fractions, and amino acid analysis of histone fractions, was performed. In untreated pernicious anemia proerythroblasts and megaloblasts, there was a small uptake of arginine and lysine as seen radioautographically, and incorporation into isolated histone fractions was scant. Amino acid analyses showed these histones to be lysine rich. After these erythroid precursors were exposed to cyanocobalamin in vivo or to coenzyme B12 in vitro, there was a marked (up to 100-fold) incorporation of only tritium-labeled L-arginine into erythroid nuclei, as seen radioautographically, and into isolated histone fractions as well. Amino acid analyses demonstrated that the histones had become more arginine rich. These studies indicate that vitamin B12 facilitates the biosynthesis of arginine-rich histones in vitamin B12-deficient erythroid precursors.


2016 ◽  
Vol Volume 112 (Number 9/10) ◽  
Author(s):  
Susan M. Chemaly ◽  

Abstract Adenosylcobalamin (AdoCbl), or coenzyme B12, is a cofactor for enzymes important in metabolism in humans (and other mammals) and bacteria. AdoCbl contains a Co-C bond and is extremely light sensitive, but, until recently, this light sensitivity appeared to have no physiological function. Recently, AdoCbl has been found to act as cofactor for a photoreceptor protein (CarH) that controls the expression of DNA coding for transcription of the proteins needed for synthesis of carotenes in certain non-photosynthetic bacteria. In 2015, the X-ray crystal structures of two dark states of the photoreceptor protein from the bacterium Thermus thermophilus were determined: CarH bound to AdoCbl and CarH bound to a large portion of the cognate DNA operator (and AdoCbl); a light state was also determined in which CarH was bound to cobalamin in which the Co-C bond had been broken. The breaking of the Co-C bond of Ado-Cbl acts as a trigger for the regulatory switch that allows the transcription of DNA. In the two dark states AdoCbl is bound to a conserved histidine from CarH, which displaces the lower 5,6-dimethylbenzimidazole ligand of AdoCbl. In the light state the 5’-deoxyadenosyl group of AdoCbl is replaced by a second histidine from CarH, giving a bis-histidine cobalamin and 4’,5’-anhydroadenosine. Genes for B12-dependent photoreceptors are widespread in bacteria. Control of DNA transcription may represent an evolutionarily ancient function of AdoCbl, possibly pre-dating its function as a protein cofactor.


FEBS Journal ◽  
2008 ◽  
Vol 275 (23) ◽  
pp. 5960-5968 ◽  
Author(s):  
Hao-Ping Chen ◽  
Huei-Ju Hsu ◽  
Fang-Ciao Hsu ◽  
Chien-Chen Lai ◽  
Chung-Hua Hsu

1980 ◽  
Vol 35 (5) ◽  
pp. 588-593 ◽  
Author(s):  
Gerhard N. Schrauzer ◽  
Masao Hashimoto ◽  
Abdussalam Maihub

Organic radicals generated by the oxidation of aldehydes, alcohols and ethers under reducing conditions are trapped by vitamin B12r to yield substituted organocobalamins. From higher n-alkyl aldehydes, acylcobalamins are formed. With acetaldehyde, a mixture of acetylcobalamin and of methylcobalamin is obtained due to the spontaneous decarbonylation of the CH3CO· radical. From saturated alcohols, w-hydroxyalkylcobalamins are produced, while w-alkoxyalkylcobalamins are formed in the corresponding reactions with radicals generated from ethers. Maximum yields of the organocobalamins are obtained if reducing conditions are maintained during the oxidation of the organic substrates. This is conveniently achieved by using V(III) salts as the reductants and the slow addition of oxidants (e.g. of O2, H2O2, Fenton reagent, or of electrochemically generated oxidizing equivalents). With 5′-deoxyadenosine, 5′-deoxyadenosylcobalamin is formed.


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