Multi-frequency epr evidence for a binuclear cua center in cytochrome c oxidase: Studies with a 63cu- and 65cu-enriched, soluble domain of the cytochrome ba3 subunit II from thermus thermophilus

James A. Fee; Donita Sanders; Claire E. Slutter; Peter E. Doan; Roland Aasa; Martin Karpefors; Tore Vänngård

doi:10.1006/bbrc.1995.1938

Multi-frequency epr evidence for a binuclear cu_a center in cytochrome c oxidase: Studies with a ⁶³cu- and ⁶⁵cu-enriched, soluble domain of the cytochrome ba₃ subunit II from thermus thermophilus

James A. Fee^*, Donita Sanders, Claire E. Slutter, Peter E. Doan, Roland Aasa, Martin Karpefors, Tore Vänngård

^*Corresponding author for this work

Chemistry

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38 Scopus citations

Abstract

We have recorded multi-frequency EPR spectra of ⁶³Cu- and ⁶⁵Cu-labeled, water-soluble Cu_A-protein from the cytochrome ba₃ of T. thermophilus. The spectrum taken at the highest frequency (34.03 GHz) shows no hyperfine structure and is nominally axial with apparent g_z ∼2.18 and g_xy ∼2.00. The spectrum taken at the lowest frequency (3.93 GHz) shows a rich hyperfine structure. Analyses of the spectra show that the observed splitting arises from an interaction of the unpaired electron with two Cu nuclei and support the notion that Cu_A is a mixed-valent [Cu(II)/Cu(I)] complex in which the unpaired electronic spin is distributed evenly over the two Cu ions.

Original language	English (US)
Pages (from-to)	77-83
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	212
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.1995.1938
State	Published - Jul 6 1995

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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Fee, J. A., Sanders, D., Slutter, C. E., Doan, P. E., Aasa, R., Karpefors, M., & Vänngård, T. (1995). Multi-frequency epr evidence for a binuclear cu_a center in cytochrome c oxidase: Studies with a ⁶³cu- and ⁶⁵cu-enriched, soluble domain of the cytochrome ba₃ subunit II from thermus thermophilus. Biochemical and Biophysical Research Communications, 212(1), 77-83. https://doi.org/10.1006/bbrc.1995.1938

@article{b44070b28c3a411daf5b4a1522c82429,

title = "Multi-frequency epr evidence for a binuclear cua center in cytochrome c oxidase: Studies with a 63cu- and 65cu-enriched, soluble domain of the cytochrome ba3 subunit II from thermus thermophilus",

abstract = "We have recorded multi-frequency EPR spectra of 63Cu- and 65Cu-labeled, water-soluble CuA-protein from the cytochrome ba3 of T. thermophilus. The spectrum taken at the highest frequency (34.03 GHz) shows no hyperfine structure and is nominally axial with apparent gz ∼2.18 and gxy ∼2.00. The spectrum taken at the lowest frequency (3.93 GHz) shows a rich hyperfine structure. Analyses of the spectra show that the observed splitting arises from an interaction of the unpaired electron with two Cu nuclei and support the notion that CuA is a mixed-valent [Cu(II)/Cu(I)] complex in which the unpaired electronic spin is distributed evenly over the two Cu ions.",

author = "Fee, {James A.} and Donita Sanders and Slutter, {Claire E.} and Doan, {Peter E.} and Roland Aasa and Martin Karpefors and Tore V{\"a}nng{\aa}rd",

year = "1995",

month = jul,

day = "6",

doi = "10.1006/bbrc.1995.1938",

language = "English (US)",

volume = "212",

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journal = "Biochemical and Biophysical Research Communications",

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Fee, JA, Sanders, D, Slutter, CE, Doan, PE, Aasa, R, Karpefors, M & Vänngård, T 1995, 'Multi-frequency epr evidence for a binuclear cu_a center in cytochrome c oxidase: Studies with a ⁶³cu- and ⁶⁵cu-enriched, soluble domain of the cytochrome ba₃ subunit II from thermus thermophilus', Biochemical and Biophysical Research Communications, vol. 212, no. 1, pp. 77-83. https://doi.org/10.1006/bbrc.1995.1938

Multi-frequency epr evidence for a binuclear cu_a center in cytochrome c oxidase: Studies with a ⁶³cu- and ⁶⁵cu-enriched, soluble domain of the cytochrome ba₃ subunit II from thermus thermophilus. / Fee, James A.; Sanders, Donita; Slutter, Claire E. et al.
In: Biochemical and Biophysical Research Communications, Vol. 212, No. 1, 06.07.1995, p. 77-83.

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

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T1 - Multi-frequency epr evidence for a binuclear cua center in cytochrome c oxidase

T2 - Studies with a 63cu- and 65cu-enriched, soluble domain of the cytochrome ba3 subunit II from thermus thermophilus

AU - Fee, James A.

AU - Sanders, Donita

AU - Slutter, Claire E.

AU - Doan, Peter E.

AU - Aasa, Roland

AU - Karpefors, Martin

AU - Vänngård, Tore

PY - 1995/7/6

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N2 - We have recorded multi-frequency EPR spectra of 63Cu- and 65Cu-labeled, water-soluble CuA-protein from the cytochrome ba3 of T. thermophilus. The spectrum taken at the highest frequency (34.03 GHz) shows no hyperfine structure and is nominally axial with apparent gz ∼2.18 and gxy ∼2.00. The spectrum taken at the lowest frequency (3.93 GHz) shows a rich hyperfine structure. Analyses of the spectra show that the observed splitting arises from an interaction of the unpaired electron with two Cu nuclei and support the notion that CuA is a mixed-valent [Cu(II)/Cu(I)] complex in which the unpaired electronic spin is distributed evenly over the two Cu ions.

AB - We have recorded multi-frequency EPR spectra of 63Cu- and 65Cu-labeled, water-soluble CuA-protein from the cytochrome ba3 of T. thermophilus. The spectrum taken at the highest frequency (34.03 GHz) shows no hyperfine structure and is nominally axial with apparent gz ∼2.18 and gxy ∼2.00. The spectrum taken at the lowest frequency (3.93 GHz) shows a rich hyperfine structure. Analyses of the spectra show that the observed splitting arises from an interaction of the unpaired electron with two Cu nuclei and support the notion that CuA is a mixed-valent [Cu(II)/Cu(I)] complex in which the unpaired electronic spin is distributed evenly over the two Cu ions.

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Multi-frequency epr evidence for a binuclear cu_a center in cytochrome c oxidase: Studies with a ⁶³cu- and ⁶⁵cu-enriched, soluble domain of the cytochrome ba₃ subunit II from thermus thermophilus

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