The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes
The in vivo experiments show that the adenosylcobalamin cofactor in glutamate mutase and methylmalonyl-CoA mutase processes lose its dimethylbenzimidazole axial ligand before starting the enzymatic processes. Complete active space self-consistent field geometry optimization of the vitamin B12 active...
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| Format: | Article |
| Language: | English |
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Academy of Sciences of Moldova, Institute of Chemistry
2023-12-01
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| Series: | Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry |
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| Online Access: |
http://cjm.ichem.md/the-co-n-bond-cleavage-in-the-adenosyncobalamin-cofactor-in-advance-to-glutamate-mutase-and-methylmalonyl-coa-mutase-processes
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| _version_ | 1827394766911832064 |
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| author | Tudor Spataru |
| author_facet | Tudor Spataru |
| author_sort | Tudor Spataru |
| collection | DOAJ |
| description | The in vivo experiments show that the adenosylcobalamin cofactor in glutamate mutase and methylmalonyl-CoA mutase processes lose its dimethylbenzimidazole axial ligand before starting the enzymatic processes. Complete active space self-consistent field geometry optimization of the vitamin B12 active forms plus substrates joint models have been performed. These joint models include the adenosylcobalamin cofactor, the carboxyl negative ion model of the studied processes’ active substrates, and the histidine molecule. Partial electronic density is transferred from the highest occupied substrate molecular orbitals to the lowest unoccupied antibonding molecular orbitals, which consist of corrin ring and dimethylbenzimidazole ligand common molecular orbitals during the multi-configurational self-consistent field molecular orbital mixing process. As a result, the Co-N axial bond is permanently elongated during the complete active space self-consistent field geometry optimization until its complete rupture and until the removal of the dimethylbenzimidazole ligand from the central cobalt atom and the corrin ring is complete. The Co-N bond cleavage in the adenosylcobalamin cofactors in the studied processes is running as no energy barrier process under the influence of their active substrates and histidine molecule. |
| first_indexed | 2024-03-08T18:17:52Z |
| format | Article |
| id | doaj.art-ab3c6b9d14ef4e7f8e193c76b47ba1c7 |
| institution | Directory Open Access Journal |
| issn | 1857-1727 2345-1688 |
| language | English |
| last_indexed | 2024-03-08T18:17:52Z |
| publishDate | 2023-12-01 |
| publisher | Academy of Sciences of Moldova, Institute of Chemistry |
| record_format | Article |
| series | Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry |
| spelling | doaj.art-ab3c6b9d14ef4e7f8e193c76b47ba1c72023-12-31T08:40:23ZengAcademy of Sciences of Moldova, Institute of ChemistryChemistry Journal of Moldova: General, Industrial and Ecological Chemistry1857-17272345-16882023-12-011829610410.19261/cjm.2023.10871087The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processesTudor Spataru0 Department of Chemistry, Columbia University, 3000, Broadway, New York, New York 10027, USA The in vivo experiments show that the adenosylcobalamin cofactor in glutamate mutase and methylmalonyl-CoA mutase processes lose its dimethylbenzimidazole axial ligand before starting the enzymatic processes. Complete active space self-consistent field geometry optimization of the vitamin B12 active forms plus substrates joint models have been performed. These joint models include the adenosylcobalamin cofactor, the carboxyl negative ion model of the studied processes’ active substrates, and the histidine molecule. Partial electronic density is transferred from the highest occupied substrate molecular orbitals to the lowest unoccupied antibonding molecular orbitals, which consist of corrin ring and dimethylbenzimidazole ligand common molecular orbitals during the multi-configurational self-consistent field molecular orbital mixing process. As a result, the Co-N axial bond is permanently elongated during the complete active space self-consistent field geometry optimization until its complete rupture and until the removal of the dimethylbenzimidazole ligand from the central cobalt atom and the corrin ring is complete. The Co-N bond cleavage in the adenosylcobalamin cofactors in the studied processes is running as no energy barrier process under the influence of their active substrates and histidine molecule. http://cjm.ichem.md/the-co-n-bond-cleavage-in-the-adenosyncobalamin-cofactor-in-advance-to-glutamate-mutase-and-methylmalonyl-coa-mutase-processes dglutamate mutasemethylmalonyl-coa mutaseadenosylcobalamin cofactorvitamin b12pseudo-jahn-teller effect |
| spellingShingle | Tudor Spataru The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry dglutamate mutase methylmalonyl-coa mutase adenosylcobalamin cofactor vitamin b12 pseudo-jahn-teller effect |
| title | The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes |
| title_full | The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes |
| title_fullStr | The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes |
| title_full_unstemmed | The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes |
| title_short | The Co-N bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl-CoA mutase processes |
| title_sort | co n bond cleavage in the adenosyncobalamin cofactor in advance to glutamate mutase and methylmalonyl coa mutase processes |
| topic | dglutamate mutase methylmalonyl-coa mutase adenosylcobalamin cofactor vitamin b12 pseudo-jahn-teller effect |
| url |
http://cjm.ichem.md/the-co-n-bond-cleavage-in-the-adenosyncobalamin-cofactor-in-advance-to-glutamate-mutase-and-methylmalonyl-coa-mutase-processes
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| work_keys_str_mv | AT tudorspataru theconbondcleavageintheadenosyncobalamincofactorinadvancetoglutamatemutaseandmethylmalonylcoamutaseprocesses AT tudorspataru conbondcleavageintheadenosyncobalamincofactorinadvancetoglutamatemutaseandmethylmalonylcoamutaseprocesses |