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Reductive activation and structural rearrangement in superoxide reductase: A combined infrared spectroscopic and computational study

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Reductive activation and structural rearrangement in superoxide reductase : A combined infrared spectroscopic and computational study. / Horch, M.; Pinto, A. F.; Utesch, T.; Mroginski, M. A.; Romão, C. V.; Teixeira, M.; Hildebrandt, P.; Zebger, I.

In: Physical chemistry chemical physics , Vol. 16, No. 27, 21.07.2014, p. 14220-14230.

Research output: Contribution to journalArticlepeer-review

Harvard

Horch, M, Pinto, AF, Utesch, T, Mroginski, MA, Romão, CV, Teixeira, M, Hildebrandt, P & Zebger, I 2014, 'Reductive activation and structural rearrangement in superoxide reductase: A combined infrared spectroscopic and computational study', Physical chemistry chemical physics , vol. 16, no. 27, pp. 14220-14230. https://doi.org/10.1039/c4cp00884g

APA

Horch, M., Pinto, A. F., Utesch, T., Mroginski, M. A., Romão, C. V., Teixeira, M., Hildebrandt, P., & Zebger, I. (2014). Reductive activation and structural rearrangement in superoxide reductase: A combined infrared spectroscopic and computational study. Physical chemistry chemical physics , 16(27), 14220-14230. https://doi.org/10.1039/c4cp00884g

Vancouver

Horch M, Pinto AF, Utesch T, Mroginski MA, Romão CV, Teixeira M et al. Reductive activation and structural rearrangement in superoxide reductase: A combined infrared spectroscopic and computational study. Physical chemistry chemical physics . 2014 Jul 21;16(27):14220-14230. https://doi.org/10.1039/c4cp00884g

Author

Horch, M. ; Pinto, A. F. ; Utesch, T. ; Mroginski, M. A. ; Romão, C. V. ; Teixeira, M. ; Hildebrandt, P. ; Zebger, I. / Reductive activation and structural rearrangement in superoxide reductase : A combined infrared spectroscopic and computational study. In: Physical chemistry chemical physics . 2014 ; Vol. 16, No. 27. pp. 14220-14230.

Bibtex - Download

@article{a95019b23f79449c8e1a7c59f26d482e,
title = "Reductive activation and structural rearrangement in superoxide reductase: A combined infrared spectroscopic and computational study",
abstract = "Superoxide reductases (SOR) are a family of non-heme iron enzymes that limit oxidative stress by catalysing the reduction of superoxide to hydrogen peroxide and, thus, represent model systems for the detoxification of reactive oxygen species. In several enzymes of this type, reductive activation of the active site involves the reversible dissociation of a glutamate from the proposed substrate binding site at the iron. In this study we have employed IR spectroscopic and theoretical methods to gain insights into redox-linked structural changes of 1Fe-type superoxide reductases, focusing on the enzyme from the archaeon Ignicoccus hospitalis. Guided by crystal structure data and complemented by spectra calculation for an active site model, the main IR difference signals could be assigned. These signals reflect redox-induced structural changes in the first coordination sphere of the iron centre, adjacent loop and helical regions, and more remote β-sheets. By comparison with the spectra obtained for the E23A mutant of Ignicoccus hospitalis SOR, it is shown that glutamate E23 dissociates reversibly from the ferrous iron during reductive activation of the wild type enzyme. Moreover, this process is found to trigger a global conformational transition of the protein that is strictly dependent on the presence of E23. Similar concerted structural changes can be inferred from the IR spectra of related SORs such as that from Archaeoglobus fulgidus, indicating a widespread mechanism. A possible functional role of this process in terms of synergistic effects during reductive activation of the homotetrameric enzyme is proposed. This journal is",
author = "M. Horch and Pinto, {A. F.} and T. Utesch and Mroginski, {M. A.} and Rom{\~a}o, {C. V.} and M. Teixeira and P. Hildebrandt and I. Zebger",
year = "2014",
month = jul,
day = "21",
doi = "10.1039/c4cp00884g",
language = "English",
volume = "16",
pages = "14220--14230",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "The Royal Society of Chemistry",
number = "27",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Reductive activation and structural rearrangement in superoxide reductase

T2 - A combined infrared spectroscopic and computational study

AU - Horch, M.

AU - Pinto, A. F.

AU - Utesch, T.

AU - Mroginski, M. A.

AU - Romão, C. V.

AU - Teixeira, M.

AU - Hildebrandt, P.

AU - Zebger, I.

PY - 2014/7/21

Y1 - 2014/7/21

N2 - Superoxide reductases (SOR) are a family of non-heme iron enzymes that limit oxidative stress by catalysing the reduction of superoxide to hydrogen peroxide and, thus, represent model systems for the detoxification of reactive oxygen species. In several enzymes of this type, reductive activation of the active site involves the reversible dissociation of a glutamate from the proposed substrate binding site at the iron. In this study we have employed IR spectroscopic and theoretical methods to gain insights into redox-linked structural changes of 1Fe-type superoxide reductases, focusing on the enzyme from the archaeon Ignicoccus hospitalis. Guided by crystal structure data and complemented by spectra calculation for an active site model, the main IR difference signals could be assigned. These signals reflect redox-induced structural changes in the first coordination sphere of the iron centre, adjacent loop and helical regions, and more remote β-sheets. By comparison with the spectra obtained for the E23A mutant of Ignicoccus hospitalis SOR, it is shown that glutamate E23 dissociates reversibly from the ferrous iron during reductive activation of the wild type enzyme. Moreover, this process is found to trigger a global conformational transition of the protein that is strictly dependent on the presence of E23. Similar concerted structural changes can be inferred from the IR spectra of related SORs such as that from Archaeoglobus fulgidus, indicating a widespread mechanism. A possible functional role of this process in terms of synergistic effects during reductive activation of the homotetrameric enzyme is proposed. This journal is

AB - Superoxide reductases (SOR) are a family of non-heme iron enzymes that limit oxidative stress by catalysing the reduction of superoxide to hydrogen peroxide and, thus, represent model systems for the detoxification of reactive oxygen species. In several enzymes of this type, reductive activation of the active site involves the reversible dissociation of a glutamate from the proposed substrate binding site at the iron. In this study we have employed IR spectroscopic and theoretical methods to gain insights into redox-linked structural changes of 1Fe-type superoxide reductases, focusing on the enzyme from the archaeon Ignicoccus hospitalis. Guided by crystal structure data and complemented by spectra calculation for an active site model, the main IR difference signals could be assigned. These signals reflect redox-induced structural changes in the first coordination sphere of the iron centre, adjacent loop and helical regions, and more remote β-sheets. By comparison with the spectra obtained for the E23A mutant of Ignicoccus hospitalis SOR, it is shown that glutamate E23 dissociates reversibly from the ferrous iron during reductive activation of the wild type enzyme. Moreover, this process is found to trigger a global conformational transition of the protein that is strictly dependent on the presence of E23. Similar concerted structural changes can be inferred from the IR spectra of related SORs such as that from Archaeoglobus fulgidus, indicating a widespread mechanism. A possible functional role of this process in terms of synergistic effects during reductive activation of the homotetrameric enzyme is proposed. This journal is

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U2 - 10.1039/c4cp00884g

DO - 10.1039/c4cp00884g

M3 - Article

C2 - 24912395

AN - SCOPUS:84902682949

VL - 16

SP - 14220

EP - 14230

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

SN - 1463-9076

IS - 27

ER -