Metal-metal bonding in biology

EXAFS evidence for a 2.5 Å copper-copper bond in the Cua center of cytochrome oxidase

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Abstract

Evidence for a direct Cu-Cu bond in the CUA center of cytochrome oxidase is reported. Simulation of the X-ray absorption spectrum of a recombirtant CuA-binding domain of Bacillus subtilis cytochrome oxidase, and comparison with a structurally characterized directly-bonding Cu(1.5)...Cu(1.5) inorganic complex, suggests that a Cu-Cu interaction of 2.5 ± 0.1 Å together with a short 2.2 Å Cu-S interaction may be present in the CuA site. In light of these data, previous interpretations of the EXAFS of a number of cytochrome oxidase and nitrous oxide reductase enzymes which modeled the 2.6 Å interaction as a long Cu-S(methionine) bond are possibly incorrect. A structural model based on the new data is presented which suggests that the CuA sites in cytochrome oxidase and N2O reductase are likely composed of a pair of modified type 1 copper centers with one histidine, one cysteine, and one weakly bound ligand (Met and/or Gln) joined by a Cu-Cu bond.

Original languageEnglish (US)
Pages (from-to)10401-10407
Number of pages7
JournalBiochemistry®
Volume33
Issue number34
StatePublished - 1994

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Electron Transport Complex IV
Copper
Metals
Structural Models
X ray absorption
Bacilli
Bacillus subtilis
Histidine
Methionine
Cysteine
Absorption spectra
Oxidoreductases
X-Rays
Ligands
Enzymes

ASJC Scopus subject areas

  • Biochemistry

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Metal-metal bonding in biology : EXAFS evidence for a 2.5 Å copper-copper bond in the Cua center of cytochrome oxidase. / Blackburn, Ninian.

In: Biochemistry®, Vol. 33, No. 34, 1994, p. 10401-10407.

Research output: Contribution to journalArticle

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abstract = "Evidence for a direct Cu-Cu bond in the CUA center of cytochrome oxidase is reported. Simulation of the X-ray absorption spectrum of a recombirtant CuA-binding domain of Bacillus subtilis cytochrome oxidase, and comparison with a structurally characterized directly-bonding Cu(1.5)...Cu(1.5) inorganic complex, suggests that a Cu-Cu interaction of 2.5 ± 0.1 {\AA} together with a short 2.2 {\AA} Cu-S interaction may be present in the CuA site. In light of these data, previous interpretations of the EXAFS of a number of cytochrome oxidase and nitrous oxide reductase enzymes which modeled the 2.6 Å interaction as a long Cu-S(methionine) bond are possibly incorrect. A structural model based on the new data is presented which suggests that the CuA sites in cytochrome oxidase and N2O reductase are likely composed of a pair of modified type 1 copper centers with one histidine, one cysteine, and one weakly bound ligand (Met and/or Gln) joined by a Cu-Cu bond.",
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