The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (CuA) and of the Heterobinuclear Fea3‐CuB Center

Gerald Henkel; Arnd Müller; Stefan Weissgräber; Gerhard Buse; Tewfik Soulimane; Guy C.M. Steffens; Hans‐Friedrich ‐F Nolting

doi:10.1002/anie.199514881

The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu_A) and of the Heterobinuclear Fe_a3‐Cu_B Center

Gerald Henkel, Arnd Müller, Stefan Weissgräber, Gerhard Buse, Tewfik Soulimane, Guy C.M. Steffens, Hans‐Friedrich ‐F Nolting

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

Abstract

A novel homobinuclear Cu₂ complex describes best the Cu_A center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fe_a3‐Cu_B center was likewise determined. (Figure Presented.)

Original language	English
Pages (from-to)	1488-1492
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	34
Issue number	13-14
DOIs	https://doi.org/10.1002/anie.199514881
Publication status	Published - 31 Jul 1995
Externally published	Yes

Keywords

X‐ray absorption spectroscopy
cytochrome‐c oxidase
metalloenzymes

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Henkel, G., Müller, A., Weissgräber, S., Buse, G., Soulimane, T., Steffens, G. C. M., & Nolting, HF. F. (1995). The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu_A) and of the Heterobinuclear Fe_a3‐Cu_B Center. Angewandte Chemie - International Edition, 34(13-14), 1488-1492. https://doi.org/10.1002/anie.199514881

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title = "The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (CuA) and of the Heterobinuclear Fea3‐CuB Center",

abstract = "A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 {\AA} is very short. The structure of the Fea3‐CuB center was likewise determined. (Figure Presented.)",

keywords = "X‐ray absorption spectroscopy, cytochrome‐c oxidase, metalloenzymes",

author = "Gerald Henkel and Arnd M{\"u}ller and Stefan Weissgr{\"a}ber and Gerhard Buse and Tewfik Soulimane and Steffens, {Guy C.M.} and Nolting, {Hans‐Friedrich ‐F}",

year = "1995",

month = jul,

day = "31",

doi = "10.1002/anie.199514881",

language = "English",

volume = "34",

pages = "1488--1492",

journal = "Angewandte Chemie - International Edition",

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Henkel, G, Müller, A, Weissgräber, S, Buse, G, Soulimane, T, Steffens, GCM & Nolting, HFF 1995, 'The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu_A) and of the Heterobinuclear Fe_a3‐Cu_B Center', Angewandte Chemie - International Edition, vol. 34, no. 13-14, pp. 1488-1492. https://doi.org/10.1002/anie.199514881

The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu_A) and of the Heterobinuclear Fe_a3‐Cu_B Center. / Henkel, Gerald; Müller, Arnd; Weissgräber, Stefan et al.
In: Angewandte Chemie - International Edition, Vol. 34, No. 13-14, 31.07.1995, p. 1488-1492.

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

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AU - Buse, Gerhard

AU - Soulimane, Tewfik

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N2 - A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fea3‐CuB center was likewise determined. (Figure Presented.)

AB - A novel homobinuclear Cu2 complex describes best the CuA center of the cytochrome‐c oxidase from bovine heart mitochondria according to EXAFS investigations. In this complex, which contains two terminal histidine residues, two cysteine sulfur bridges, and probably a bridging oxygen donor function, the CuCu distance of 2.46 Å is very short. The structure of the Fea3‐CuB center was likewise determined. (Figure Presented.)

KW - X‐ray absorption spectroscopy

KW - cytochrome‐c oxidase

KW - metalloenzymes

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Henkel G, Müller A, Weissgräber S, Buse G, Soulimane T, Steffens GCM et al. The Active Sites of the Native Cytochrome‐c Oxidase from Bovine Heart Mitochondria: EXAFS‐Spectroscopic Characterization of a Novel Homobinuclear Copper Center (Cu_A) and of the Heterobinuclear Fe_a3‐Cu_B Center. Angewandte Chemie - International Edition. 1995 Jul 31;34(13-14):1488-1492. doi: 10.1002/anie.199514881