Model Studies for the Methylmalonyl‐Succinyl Rearrangement

Keese, Reinhart; Darbre, Tamis; v., Urs; Miiller, Susanna; Wolleb-Gygi, Annemarie; Hirschi, Daniel; Siljegovic, Vuk; Hammatter, Michael; Amolins, Andris; Otten, Thomas

doi:10.1002/9783527612192.ch19

Cited by 3 publications

(1 citation statement)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For models of vitamin B12 (B12; Figure 1), the study of `incomplete` corrinoids lacking the intramolecularly bound dimethylbenzimidazole base (Dmbz) at the f-side chain such as dicyano-, and aquacyanocobinamides (Cbi) 1 and 2 + (Figure 2A) gave important insights into properties and reactivity of Co-containing corrin macrocycles. [4][5][6][7][8][9][10] A variety of more sophisticated cobalamin (Cbl)-protein models have then been prepared by the groups of Rétey, 11,12 Golding, 13,14 Darbre and Keese [15][16][17] , Hisaeda, 18,19 , Hayashi 20,21 and others [22][23][24][25][26][27] to yield insights into B12-catalyzed enzymatic reactions.…”

Section: Introductionmentioning

confidence: 99%

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Sonnay

Zelder

2018

Dalton Trans.

View full text Add to dashboard Cite

This communication describes the stabilizing effect (ΔΔG° = -4 kJ mol) of a remote methyl group in the backbone of a cobalamin-enzyme mimic on intramolecular imidazole-cobalt coordination. For this purpose, two B derivatives with an appended imidazole base were synthesized and analysed with spectrophotometric pH titrations. Qualitative conformation analysis of the backbone structure suggests that a thermodynamically unfavoured gauche interaction in the base-off form of a model containing an (R)-configured CH group at position C176 of the linker between the corrin ring and the terminal imidazole ligand steers the base toward cobalt coordination.

show abstract

Section: Introductionmentioning

confidence: 99%

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Sonnay

Zelder

2018

Dalton Trans.

View full text Add to dashboard Cite

show abstract

Cobalt Enzymes/Models

Kräutler

2010

Encyclopedia of Catalysis

View full text Add to dashboard Cite

Vitamin B 12 and its coenzyme forms are prominent cobalt‐containing cofactors and part of the larger class of the natural tetrapyrrolic metal complexes. Such cobalt corrinoids are an important component of human nutrition, and many (other) forms of life also depend upon them. Cobalt‐containing corrinoid cofactors play basic roles in carbon fixation and energy metabolism in anaerobes, as well as in the carbon metabolism in a broad range of lower organisms. Microorganisms developed unique B 12 biosynthetic means and, indeed, are the only natural sources of the B 12 derivatives. Other organisms have evolved intricate strategies for the uptake and transport of the corrinoids. The cofactor functions of cobalt corrinoids are a result of their extraordinary organometallic chemistry under physiological conditions and their redox chemistry. Coenzyme B 12 (a reversible source of a free radical), methylcobalamin (a versatile methylating agent), and reduced (supernucleophilic or radicaloid) corrinoids are cofactors in a range of enzymes. These enzymes channel the specific reactivity of B 12 cofactors into biological catalysis of unique reactions, involving radicals and organometallic intermediates. B 12 ‐dependent enzymes thus pose still puzzling structural and mechanistic questions, as does the recently discovered interaction of B 12 cofactors with RNA.

show abstract

Vitamin B₁₂and Heme Models

Doorslaer¹

2004

Encyclopedia of Supramolecular Chemistry

View full text Add to dashboard Cite

Model Studies for the Methylmalonyl‐Succinyl Rearrangement

Cited by 3 publications

References 25 publications

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Cobalt Enzymes/Models

Vitamin B₁₂and Heme Models

Contact Info

Product

Resources

About

Model Studies for the Methylmalonyl‐Succinyl Rearrangement

Cited by 3 publications

References 25 publications

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B12–protein model

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B12–protein model

Cobalt Enzymes/Models

Vitamin B12and Heme Models

Contact Info

Product

Resources

About

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B₁₂–protein model

Vitamin B₁₂and Heme Models