The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Vitamin B12-derivatives—enzyme cofactors and ligands of proteins and nucleic acids
Abstract
B(12)-cofactors play important roles in the metabolism of microorganisms, animals and humans. Microorganisms are the only natural sources of B(12)-derivatives, and the latter are "vitamins" for other B(12)-requiring organisms. Some B(12)-dependent enzymes catalyze complex isomerisation reactions, such as methylmalonyl-CoA mutase. They need coenzyme B(12), an organometallic B(12)-derivative, to induce enzymatic radical reactions. Another group of widely relevant enzymes catalyzes the transfer of methyl groups, such as methionine synthase, which uses methylcobalamin as cofactor. This tutorial review covers structure and reactivity of B(12)-derivatives and structural aspects of their interactions with proteins and nucleotides, which are crucial for the efficient catalysis by the important B(12)-dependent enzymes, and for achieving and regulating uptake and transport of B(12)-derivatives.
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Citations
Cites
Vitamin B12: Experiments Concerning the Origin of Its Molecular Structure
Eschenmoser, A. (1988) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198800051 · Cited by 374
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Zhang, P., & Sadler, P. J. (2017) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2017.03.038 · Cited by 369
Vitamin B12catalysed reactions
Giedyk, M., Goliszewska, K., & Gryko, D. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00165j · Cited by 340
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Del Mondo, A., Smerilli, A., Sané, E., Sansone, C., & Brunet, C. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01459-1 · Cited by 220
Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer
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Metadata
- Authors
- Gruber, K., Puffer, B., & Kräutler, B.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2011
- Volume
- 40
- Issue
- 8
- Pages
- 4346
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2083400700
- Cited by
- 272
- References
- 1
- FWCI
- 0.97
- Type
- journal article
- Language
- en
- Open access
- closed
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