The Cu_A Center of a Soluble Domain from Thermus Cytochrome ba_3. An NMR Investigation of the Paramagnetic Protein
Creators
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1.
University of Gothenburg
Abstract
The Cu_A center in subunit II of cytochrome c oxidase, the terminal enzyme of aerobic respiration, transfers electrons from cytochrome c to the proton-pumping machinery in subunit I. The unique electronic absorption and EPR spectra of Cu_A exclude it from classification with the well-studied biological copper centers. High-resolution X-ray structures of Cu_A-containing proteins reveal two copper atoms approximately 2.5 Å apart, bridged by two cysteine sulfurs. Each Cu has a terminal histidine ligand and a weak ligand, methionine for one and a main chain carbonyl for the other. These structures are consistent with earlier EPR measurements and theoretical calculations, which predicted a highly delocalized mixed-valence [Cu(II),Cu(I)] Cu_A site. Here we report ^1H NMR measurements at 600 MHz on a soluble Cu_A domain from Thermus thermophilus cytochrome ba_3.
Additional Information
© 1996 American Chemical Society. Received June 25, 1996. Publication Date (Web): November 20, 1996. Support from NIH (J.A.F., GM 35342; H.B.G., DK 19038; J.H.R., GM 16424) is acknowledged. B.G.M. is grateful to the FLORMARPARM Large Scale Facility of the EU, which supported his stay in Florence. The University of Florence is acknowledged for partially supporting C.E.S. and J.H.R. in Florence. Supporting Information Available: A 4 ms 2D NOESY spectrum at pH 4.5 and 278 K (2 pages).Attached Files
Supplemental Material - ja11658.pdf
Files
ja11658.pdf
Additional details
Identifiers
- Eprint ID
- 57197
- Resolver ID
- CaltechAUTHORS:20150504-120953603
Funding
- NIH
- GM 35342
- NIH
- DK 19038
- NIH
- GM 16424
- FLORMARPARM Large Scale Facility
- University of Florence
Dates
- Created
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2015-05-04Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field