Investigation of the Mn binding site in cytochrome c oxidase from Paracoccus denitrificans by high-frequency EPR

Kass, H., Macmillan, F., Ludwig, B. and Prisner, T. F. (2000) Investigation of the Mn binding site in cytochrome c oxidase from Paracoccus denitrificans by high-frequency EPR. The Journal of Physical Chemistry B, 104 (22). pp. 5362-5371. ISSN 1089-5647

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Abstract

Cytochrome c oxidase contains a redox-inactive metal center of unknown function. It has been shown that for Paracocccus denitrificans, depending on growth conditions, Mn2+ ions can occupy the Mg2+ site in the functional protein. Differences between the 9.5 GHz X-band electron paramagnetic resonance (EPR) spectra of such Mn2+ preparations in oxidized and reduced state have previously been interpreted as being due to conformational changes. However, only minor differences have been found in analogous 34 GHz Q-band EPR experiments on Mn2+ containing cytochrome c oxidase from Rhodobacter sphaeroides. The new temperature-dependent X-, Q- and 95 GHz W-band EPR data from Paracoccus preparations shown here provide a consistent explanation of these contrasting former interpretations. The EPR spectra of oxidized samples reveal contributions of a dipolar interaction between the Mn2+ spin and the paramagnetic dinuclear Cu-A center. In reduced samples, the Cu-A center is diamagnetic, and thus, a pure Mn2+ signal is found. The zerofield parameters D and E are 145 +/- 10 (120 +/- 5) G and 28 +/- 5 (22 +/- 3) G in the fury oxidized (reduced) protein. From the evaluated dipolar coupling constant of 33.6 +/- 1 G, an averaged distance between Mn2+ and the Cu-A center of 9.4 +/- 0.2 Angstrom was calculated, providing an independent confirmation of the distance calculated from the 2.7 Angstrom X-ray structure.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
University of East Anglia > Faculty of Science > Research Groups > Biophysical Chemistry
Depositing User: Rachel Smith
Date Deposited: 19 Jul 2011 12:00
Last Modified: 25 Jul 2018 07:55
URI: https://ueaeprints.uea.ac.uk/id/eprint/33883
DOI:

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