NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native FesupII/supOinf2/infReaction

0489343 - ÚFCH JH 2019 RIV US eng J - Článek v odborném periodiku
Sutherlin, K. D. - Rivard, B. S. - Böttger, L. H. - Liu, L. V. - Rogers, M. S. - Srnec, Martin - Park, K. - Yoda, Y. - Kitao, S. - Kobayashi, Y. - Saito, M. - Seto, M. - Hu, M. - Zhao, J. - Lipscomb, J. D. - Solomon, E. I.
NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native FesupII/supOinf2/infReaction.
Journal of the American Chemical Society. Roč. 140, č. 16 (2018), s. 5544-5559. ISSN 0002-7863. E-ISSN 1520-5126
Institucionální podpora: RVO:61388955
Klíčová slova: NRVS studies * Rieske dioxygenase * mononuclear nonheme iron enzymes
Obor OECD: Physical chemistry
Impakt faktor: 14.695, rok: 2018

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.
Trvalý link: http://hdl.handle.net/11104/0283781