The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry
The ability of enzymes to harness free-radical chemistry allows for some of the most amazing transformations in nature, including reduction of ribonucleotides and carbon skeleton rearrangements. Enzyme cofactors involved in this chemistry can be large and complex, such as adenosylcobalamin (coenzyme...
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| Format: | Article |
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Annual Reviews
2012
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| Online Access: | http://hdl.handle.net/1721.1/74068 https://orcid.org/0000-0001-5486-2755 |
| _version_ | 1826202002759090176 |
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| author | Dowling, Daniel P. Croft, Anna K. Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Dowling, Daniel P. Croft, Anna K. Drennan, Catherine L |
| author_sort | Dowling, Daniel P. |
| collection | MIT |
| description | The ability of enzymes to harness free-radical chemistry allows for some of the most amazing transformations in nature, including reduction of ribonucleotides and carbon skeleton rearrangements. Enzyme cofactors involved in this chemistry can be large and complex, such as adenosylcobalamin (coenzyme B[subscript 12]), simpler, such as S-adenosylmethionine and an iron-sulfur cluster (i.e., poor man's B[subscript 12]), or very small, such as one nonheme iron atom coordinated by protein ligands. Although the chemistry catalyzed by these enzyme-bound cofactors is unparalleled, it does come at a price. The enzyme must be able to control these radical reactions, preventing unwanted chemistry and protecting the enzyme active site from damage. Here, we consider a set of radical folds: the (β/α)8 or TIM barrel, combined with a Rossmann domain for coenzyme B[subscript 12]-dependent chemistry. Using specific enzyme examples, we consider how nature employs the common TIM barrel fold and its Rossmann domain partner for radical-based chemistry. |
| first_indexed | 2024-09-23T12:00:19Z |
| format | Article |
| id | mit-1721.1/74068 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T12:00:19Z |
| publishDate | 2012 |
| publisher | Annual Reviews |
| record_format | dspace |
| spelling | mit-1721.1/740682024-03-21T20:13:49Z The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry Dowling, Daniel P. Croft, Anna K. Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Drennan, Catherine L. Dowling, Daniel P. Drennan, Catherine L. The ability of enzymes to harness free-radical chemistry allows for some of the most amazing transformations in nature, including reduction of ribonucleotides and carbon skeleton rearrangements. Enzyme cofactors involved in this chemistry can be large and complex, such as adenosylcobalamin (coenzyme B[subscript 12]), simpler, such as S-adenosylmethionine and an iron-sulfur cluster (i.e., poor man's B[subscript 12]), or very small, such as one nonheme iron atom coordinated by protein ligands. Although the chemistry catalyzed by these enzyme-bound cofactors is unparalleled, it does come at a price. The enzyme must be able to control these radical reactions, preventing unwanted chemistry and protecting the enzyme active site from damage. Here, we consider a set of radical folds: the (β/α)8 or TIM barrel, combined with a Rossmann domain for coenzyme B[subscript 12]-dependent chemistry. Using specific enzyme examples, we consider how nature employs the common TIM barrel fold and its Rossmann domain partner for radical-based chemistry. Howard Hughes Medical Institute (Investigator) National Institutes of Health (U.S.) (GM69857) National Science Foundation (U.S.) (MCB- 0543833) 2012-10-18T14:08:25Z 2012-10-18T14:08:25Z 2012-06 Article http://purl.org/eprint/type/JournalArticle 1936-122X 1936-1238 http://hdl.handle.net/1721.1/74068 Dowling, Daniel P., Anna K. Croft, and Catherine L. Drennan. “Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12]Chemistry.” Annual Review of Biophysics 41.1 (2012): 403–427. https://orcid.org/0000-0001-5486-2755 en_US http://www.annualreviews.org/doi/abs/10.1146/annurev-biophys-050511-102225 Annual Review of Biophysics Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Annual Reviews Prof. Drennan via Erja Kajosalo |
| spellingShingle | Dowling, Daniel P. Croft, Anna K. Drennan, Catherine L The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title | The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title_full | The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title_fullStr | The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title_full_unstemmed | The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title_short | The Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B[subscript 12] Chemistry |
| title_sort | radical use of rossmann and tim barrel architectures for controlling coenzyme b subscript 12 chemistry |
| url | http://hdl.handle.net/1721.1/74068 https://orcid.org/0000-0001-5486-2755 |
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