Copper electron-nuclear double resonance of cytochrome c oxidase.

B. M. Hoffman; J. E. Roberts; M. Swanson; S. H. Speck; E. Margoliash

doi:10.1073/pnas.77.3.1452

Copper electron-nuclear double resonance of cytochrome c oxidase.

B. M. Hoffman^*, J. E. Roberts, M. Swanson, S. H. Speck, E. Margoliash

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Article › peer-review

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Abstract

Electron-nuclear double resonance of copper was observed while monitoring the "intrinsic copper" electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and the maximum value is about half that seen in type I blue copper proteins. The magnetic properties of this oxidized copper center are not consistent with those of a thiyl radical (R-S) coordinated to Cu(I), and thus favor the identification of this redox center as a Cu(II) ion in a unique environment.

Original language	English (US)
Pages (from-to)	1452-1456
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	77
Issue number	3
DOIs	https://doi.org/10.1073/pnas.77.3.1452
State	Published - Mar 1980

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title = "Copper electron-nuclear double resonance of cytochrome c oxidase.",

abstract = "Electron-nuclear double resonance of copper was observed while monitoring the {"}intrinsic copper{"} electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and the maximum value is about half that seen in type I blue copper proteins. The magnetic properties of this oxidized copper center are not consistent with those of a thiyl radical (R-S) coordinated to Cu(I), and thus favor the identification of this redox center as a Cu(II) ion in a unique environment.",

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year = "1980",

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T1 - Copper electron-nuclear double resonance of cytochrome c oxidase.

AU - Hoffman, B. M.

AU - Roberts, J. E.

AU - Swanson, M.

AU - Speck, S. H.

AU - Margoliash, E.

PY - 1980/3

Y1 - 1980/3

N2 - Electron-nuclear double resonance of copper was observed while monitoring the "intrinsic copper" electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and the maximum value is about half that seen in type I blue copper proteins. The magnetic properties of this oxidized copper center are not consistent with those of a thiyl radical (R-S) coordinated to Cu(I), and thus favor the identification of this redox center as a Cu(II) ion in a unique environment.

AB - Electron-nuclear double resonance of copper was observed while monitoring the "intrinsic copper" electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and the maximum value is about half that seen in type I blue copper proteins. The magnetic properties of this oxidized copper center are not consistent with those of a thiyl radical (R-S) coordinated to Cu(I), and thus favor the identification of this redox center as a Cu(II) ion in a unique environment.

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Copper electron-nuclear double resonance of cytochrome c oxidase.

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