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Journal ArticleDOI

Structure and function of copper proteins : Report, on the fourth La Cura Conference held at Villa Giulia, Manziana, Rome, Italy, 4-8 September 1979

Helmut Beinert
- 01 Sep 1980 - 
- Vol. 33, Iss: 1, pp 55-85
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This article is published in Coordination Chemistry Reviews.The article was published on 1980-09-01. It has received 77 citations till now.

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Citations
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Journal ArticleDOI

Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values.

TL;DR: The structure of poplar plastocyanin in the reduced (CuI) state has been determined and refined, using counter data recorded from crystals at pH 3.8 and 7.8, and the trigonal geometry of the Cu atom strongly favours CuI, so that this form of the protein should be redox-inactive.
Journal ArticleDOI

Crown thio ether chemistry

Book ChapterDOI

Chemistry of Thioether Macrocyclic Complexes

TL;DR: In this paper, a summary of the coordination chemistry of homoleptic thioether macrocycles is presented, with emphasis on likely future developments and uses, and some unpublished results are discussed.
Book ChapterDOI

Crown thioether chemistry

TL;DR: In this paper, the synthesis, structural, and coordination chemistry of crown thioethers with both transition and p-block metal ions is reviewed comprehensively through December 1988, focusing on the electronic structures and redox properties induced in metal ions by coordination to crown thiosethers.
Journal ArticleDOI

Characterization of Starburst Dendrimers by the EPR Technique. Copper(II) Ions Binding Full-Generation Dendrimers

TL;DR: In this paper, computer-aided analysis of the EPR spectra provided information on the formation of copper complexes in various internal or external locations of the dendrimers, as well as the nSBD structure.
References
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Journal ArticleDOI

X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution

TL;DR: The three-dimensional structure of plastocyanin, a blue or "Type 1" copper-protein, has been determined at a resolution of 2.7 A as discussed by the authors, and it is coordinated by a cysteine thiol group, a methionine thioether group and two histidine imidazole groups.
Journal ArticleDOI

A different genetic code in human mitochondria

TL;DR: Comparison of the human mitochrondrial DNA sequence of the cytochrome oxidase subunit II gene and the sequence of a corresponding beef heart protein shows that UGA is used as a tryptophan codon and not as a termination codon, and suggests that AU A may be a methionine and not an isoleucine codon.
Journal ArticleDOI

Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase.

TL;DR: It is concluded that Physiological concentrations of ATP decrease the affinity of this binding to the point that interaction of cytochrome c with numerous mitochondrial pholpholipid sites can competitively remove cy tochrome c from the oxidase.
Journal ArticleDOI

Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen.

TL;DR: The remarkable features of cytochrome oxidase are its highly dissociable "oxy" compound and its extremely effective electron donor reaction which converts this rapidly to tightly bound reduced oxygen and oxidized oxidase.
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