ChemInform Abstract: Synthesis of the C-Ring Fragment (III) of Cobyric Acid (IV).

ChemInform ◽  
2010 ◽  
Vol 30 (42) ◽  
pp. no-no
Author(s):  
Johann Mulzer ◽  
Doris Riether
Keyword(s):  
Cobyric Acid

ChemInform Abstract: Efficient Synthesis of the D-Ring Fragment of Cobyric Acid.

ChemInform ◽  
2001 ◽  
Vol 32 (6) ◽  
pp. no-no
Author(s):  
Johann Mulzer ◽  
Doris Riether
Keyword(s):  
Efficient Synthesis ◽  
Cobyric Acid

Total synthesis of vitamin B12 — a fellowship of the ring

2016 ◽  
Vol 20 (01n04) ◽  
pp. 1-20 ◽  
Author(s):  
G. Wayne Craig
Keyword(s):  
Total Synthesis ◽  
Vitamin B12 ◽  
Cyclic Ether ◽  
Vitamin B ◽  
Porphyrin Molecule ◽  
Cobyric Acid

In the synthesis of cobyric acid following an arduous 60-step synthesis of the tetrapyrrole corrigenolide, Woodward demonstrated that ring cyclization yielded unexpectedly the corrin cyclic ether (Fig. 2). Its structure was chosen as the chemistry logo for the 1970 IUPAC meeting. It was a reminder that chemistry can be capricious and beautiful. This article is a tribute to the 50-year career in porphyrins of Professor Kevin M. Smith and describes his early contributions with colleagues in the synthetic quest of a related porphyrin molecule, vitamin B12 (Fig. 1a).

Conversion of Cobinamide into Cobyric Acid

1966 ◽  
Vol 5 (1) ◽  
pp. 125-126
Author(s):  
Gerhard Müller ◽  
Otto Müller
Keyword(s):  
Cobyric Acid

scholarly journals Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of sirohaem synthase (CysG) on sirohaem and cobalamin biosynthesis

1998 ◽  
Vol 330 (1) ◽  
pp. 121-129 ◽  
Author(s):  
C. Sarah WOODCOCK ◽  
Evelyne RAUX ◽  
Florence LEVILLAYER ◽  
Claude THERMES ◽  
Alain RAMBACH ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Catalytic Domain ◽  
Conserved Residues ◽  
Pseudomonas Denitrificans ◽  
E Coli ◽  
Cobalamin Biosynthesis ◽  
N Terminus ◽  
Low Levels ◽  
Cobyric Acid

The Escherichia coli CysG protein (sirohaem synthase) catalyses four separate reactions that are required for the transformation of uroporphyrinogen III into sirohaem, initially two S-adenosyl-L-methionine-dependent transmethylations at positions 2 and 7, mediated through the C-terminal, or CysGA, catalytic domain of the protein, and subsequently a ferrochelation and dehydrogenation, mediated through the N-terminal, or CysGB, catalytic domain of the enzyme. This report describes how the deletion of the NAD+-binding site of CysG, located within the first 35 residues of the N-terminus, is detrimental to the activity of CysGB but does not affect the catalytic activity of CysGA, whereas the mutation of a number of phylogenetically conserved residues within CysGA is detrimental to the transmethylation reaction but does not affect the activity of CysGB. Further studies have shown that CysGB is not essential for cobalamin biosynthesis because the presence of the Salmonella typhimurium CobI operon with either cysGA or the Pseudomonas denitrificans cobA are sufficient for the synthesis of cobyric acid in an E. coli cysG deletion strain. Evidence is also presented to suggest that a gene within the S. typhimurium CobI operon might act as a chelatase that, at low levels of cobalt, is able to aid in the synthesis of sirohaem.

Cobyric acid and related compounds from vitamin B12

1969 ◽  
pp. 1163 ◽  
Author(s):  
R. Bonnett ◽  
J. M. Godfrey ◽  
D. G. Redman
Keyword(s):  
Vitamin B12 ◽  
Cobyric Acid ◽  
Related Compounds

Über die Darstellung sowie Elektronen-und CD-Spektren der Co(I)-Form einiger natürlicher Corrinoide / Synthesis and Spectra (Electronic, CD ) of the Co(I) Form of Several Natural Corrinoids

1979 ◽  
Vol 34 (9-10) ◽  
pp. 689-694 ◽  
Author(s):  
Matthäus Moskophidis
Keyword(s):  
Sodium Borohydride ◽  
Electronic Spectra ◽  
The Other ◽  
Cd Spectra ◽  
Cobyric Acid

Abstract Several natural corrinoids, cobalamin, 5-hydroxybenzimidazolyl cobamide (factor III), adenyl cobam ide (pseudovitam in B12), 2-methyladenyl cobamide (factor A) and cobyric acid, were reduc­ed with sodium borohydride. The reduction of cyanocobalam in is slow as compared with that of factor III and especially of the other corrinoids under study. At longer wavelengths (λ > 300 nm) the electronic spectra of the Co(I)-corrinoids are nearly identical. The same is to say about the CD-spectra of the Co(I)-corrinoids examined.

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