Copper electron-nuclear double resonance of cytochrome c oxidase. | Zendy

Brian M. Hoffman | Zendy; James E. Roberts | Zendy; Maurice S. Swanson | Zendy; Samuel H. Speck | Zendy; E. Margoliash | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Copper electron-nuclear double resonance of cytochrome c oxidase.

Author(s) -

Brian M. Hoffman,

James E. Roberts,

Maurice S. Swanson,

Samuel H. Speck,

E. Margoliash

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.3.1452

Subject(s) - copper , chemistry , electron paramagnetic resonance , redox , cytochrome c oxidase , hyperfine structure , heme a , oxygen , oxidoreductase , multicopper oxidase , nuclear magnetic resonance , photochemistry , crystallography , inorganic chemistry , mitochondrion , enzyme , atomic physics , biochemistry , physics , organic chemistry , laccase

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research