The currents of life: the terminal electron-transfer complex of respiration.

Ramirez, Benjamin E.; Malmström, Bo G.; Winkler, Jay R.; Gray, Harry B.

doi:10.1073/pnas.92.26.11949

Cited by 184 publications

(194 citation statements)

References 18 publications

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“…Copper-containing proteins and enzymes play crucial roles in metabolic and cellular processes in both eukaryotes and prokaryotes [1][2][3][4], such as electron transport (plastocyanin, azurin, stellacyanin) [5][6][7], in oxygen transport in arthropods and mollusks (hemocyanin) [8,9], in the reduction of O 2 to H 2 O [cytochrome c oxidase (COX), laccase, ascorbate oxidase] [10], in the reduction of O 2 to H 2 O 2 (amine oxidase, galactose oxidase) [11,12], in the oxidation of various organic substrates (tyrosinase, methane monooxygenase, dopamine b-hydroxylase) [12,13], and in the reduction of small inorganic molecules [nitrite reductase, nitrous oxide reductase (N 2 OR), superoxide dismutase] [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

et al. 2011

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This review focuses on the novel CuZ center of nitrous oxide reductase, an important enzyme owing to the environmental significance of the reaction it catalyzes, reduction of nitrous oxide, and the unusual nature of its catalytic center, named CuZ. The structure of the CuZ center, the unique tetranuclear copper center found in this enzyme, opened a novel area of research in metallobiochemistry. In the last decade, there has been progress in defining the structure of the CuZ center, characterizing the mechanism of nitrous oxide reduction, and identifying intermediates of this reaction. In addition, the determination of the structure of the CuZ center allowed a structural interpretation of the spectroscopic data, which was supported by theoretical calculations. The current knowledge of the structure, function, and spectroscopic characterization of the CuZ center is described here. We would like to stress that although many questions have been answered, the CuZ center remains a scientific challenge, with many hypotheses still being formed.

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Section: Introductionmentioning

confidence: 99%

The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

et al. 2011

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“…In the terminal reaction of the respiratory chain, cyt c oxidase (CcO) removes electrons from cyt c and passes them on to O 2 (80). CcO is a multisubunit membrane-bound enzyme with four redox cofactors (Cu A , cyt a, cyt a 3 , and Cu B ).…”

Section: Protein-protein Reactionsmentioning

confidence: 99%

Long-range electron transfer

Gray

Winkler

2005

Proc. Natl. Acad. Sci. U.S.A.

744

841

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Recent investigations have shed much light on the nuclear and electronic factors that control the rates of long-range electron tunneling through molecules in aqueous and organic glasses as well as through bonds in donor-bridge-acceptor complexes. Couplings through covalent and hydrogen bonds are much stronger than those across van der Waals gaps, and these differences in coupling between bonded and nonbonded atoms account for the dependence of tunneling rates on the structure of the media between redox sites in Ru-modified proteins and protein-protein complexes.electron tunneling ͉ hopping ͉ glass ͉ protein

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“…Gray and coworkers (16,17) identified a direct Cu A -to-heme a coupling pathway that would support effec- tive ET, as well as an axial-to-axial heme a-to-heme a 3 pathway. Stuchebrukhov and coworkers (18) examined the axial coupling route and also identified a direct heme-to-heme route (via methyl groups on the D rings).…”

Section: Coupling Routes and Tunneling Barriers In Cytochrome C Oxidasementioning

confidence: 99%