NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native Fe<sup>II</sup>O<inf>2</inf>Reaction
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F18%3A00489343" target="_blank" >RIV/61388955:_____/18:00489343 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/jacs.8b01822" target="_blank" >http://dx.doi.org/10.1021/jacs.8b01822</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jacs.8b01822" target="_blank" >10.1021/jacs.8b01822</a>
Alternative languages
Result language
angličtina
Original language name
NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native Fe<sup>II</sup>O<inf>2</inf>Reaction
Original language description
The Rieske dioxygenases are a major subclass of mononuclear nonheme iron enzymes that play an important role in bioremediation. Recently, a high-spin Fe III(hydro)peroxy intermediate (BZDOp) has been trapped in the peroxide shunt reaction of benzoate 1,2-dioxygenase. Defining the structure of this intermediate is essential to understanding the reactivity of these enzymes. Nuclear resonance vibrational spectroscopy (NRVS) is a recently developed synchrotron technique that is ideal for obtaining vibrational, and thus structural, information on Fe sites, as it gives complete information on all vibrational normal modes containing Fe displacement. In this study, we present NRVS data on BZDOp and assign its structure using these data coupled to experimentally calibrated density functional theory calculations. From this NRVS structure, we define the mechanism for the peroxide shunt reaction. The relevance of the peroxide shunt to the native Fe II /O 2 reaction is evaluated. For the native Fe II /O 2 reaction, an Fe IIIsuperoxo intermediate is found to react directly with substrate. This process, while uphill thermodynamically, is found to be driven by the highly favorable thermodynamics of proton-coupled electron transfer with an electron provided by the Rieske [2Fe-2S] center at a later step in the reaction. These results offer important insight into the relative reactivities of Fe IIIsuperoxo and Fe IIIhydroperoxo species in nonheme Fe biochemistry.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of the American Chemical Society
ISSN
0002-7863
e-ISSN
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Volume of the periodical
140
Issue of the periodical within the volume
16
Country of publishing house
US - UNITED STATES
Number of pages
16
Pages from-to
5544-5559
UT code for WoS article
000431095100030
EID of the result in the Scopus database
2-s2.0-85045974778