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The substrate reaction mechanism of class III anaerobic ribonucleotide reductase
2001 (English)In: Journal of Physical Chemistry B, ISSN 1089-5647, Vol. 105, no 27, 6445-6452 p.Article in journal (Refereed) Published
Abstract [en]

The substrate mechanism of class III anaerobic ribonucleotide reductase has been studied using quantum chemical methods. The study is based on the previously suggested mechanism for the aerobic class I enzyme, together with the recently determined X-ray structure of the anaerobic enzyme. The initial steps are similar in the mechanisms of these enzymes, but for the suggested rate-limiting steps there are key differences. In the class I enzyme, the 3 ' -keto group of the substrate is protonated in a step involving formation of a sulfur-sulfur bond between two cysteines, One of these cysteines is not present in the anaerobic enzyme. Instead, carbon dioxide is formed in this step from formate, which is present as a cofactor. In line with previous suggestions from experimental observations, the formate first forms a formyl radical. The next step, where the formyl radical protonates the 3 ' -keto group of the substrate, is suggested to be rate limiting with a calculated total barrier of 19.9 kcal/mol, in reasonable agreement with the experimental rate-limiting barrier of 17 kcal/mol. Zero-point and entropy effects are found to be quite significant in lowering the barrier. The mechanism for the entire cycle is discussed in relation to known experimental facts.

Place, publisher, year, edition, pages
2001. Vol. 105, no 27, 6445-6452 p.
Keyword [en]
pyruvate formate-lyase, iron-sulfur center, acid side-chains, escherichia-coli, proton-exchange, bacteriophage-t4, cysteines, radicals, energy, model
Identifiers
URN: urn:nbn:se:kth:diva-20786ISI: 000169823800024OAI: oai:DiVA.org:kth-20786DiVA: diva2:339483
Note
QC 20100525Available from: 2010-08-10 Created: 2010-08-10Bibliographically approved

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