Copper coordination in nitrous oxide reductase from Pseudomonas stutzeri

Hu, Jin; Thomann, H.; Coyle, C. L.; Zumft, Walter G.

doi:10.1021/ja00194a017

Cited by 53 publications

(38 citation statements)

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“…ENDOR data are compatible with the mixed-valence hypothesis. From electron-spin-echo studies of COX, it was inferred that the EPR-detectable site was not consistent with the tetrahedral Cu(11) model proposed by Greenaway et al (1977), or a type-1 blue Cu center (Mims et al, 1980;Jin et al, 1989).…”

Section: Discussionmentioning

confidence: 97%

“…In contrast, the EPR spectra at 2.7 GHz and 4.6 GHz are well resolved (Figs 4 -6). The EPR parameters for COX were thought to be unique until a comparison with the EPR parameters and the ESEEM data for N 2 0 R I was made (Kroneck et al, 1988;Riester et al, 1989;Jin et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…1990). This conclusion is derived from investigating both enzymes by resonance Raman (Dooley et al, 1987), magnetic CD (MCD) and extended X-ray absorption fine structure (EXAFS; Scott et al, 1989;Dooley et al, 1991 ;Farrdr et al, 1991) and electronspin-echo envelope modulation (ESEEM; Jin et al, 1989).…”

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confidence: 99%

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A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

Antholine

Kastrau

Steffens

et al. 1992

European Journal of Biochemistry

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185

170

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The multicopper proteins, nitrous-oxide reductase (N20R) and cytochrome c oxidase (COX), were investigated by EPR spectroscopy at microwave frequencies 2.4 -35 GHz. Our results support a Cu-Cu interaction in COX and N20R. At least 10 lines in the 2.7-GHz, 12 lines in the 4.6-GHz and 14 lines in the 9.2 GHz spectra were resolved for N20R. Eight copper lines at 2.7 GHz, about ninc lines at 4.6 GHz and about six lines at 9.2 G H L were resolved for COX. Simulations of the EPR spectra were consistent with most of the resonances of the multiline spectra, including regions in the center of the spectra where overlap of the three seven-line patterns is proposed. These simulations indicated that Cu-Cu interaction, in a mixed-valence [Cu(l.5). . .Cu(l.5)], S = site is consistent with, if not proof of, the unusual spectral features observed for N 2 0 R and COX.Nitrous-oxide reductase (N20R) is the terminal electron acceptor in a respiratory chain converting N 2 0 to N2 in denitrifying bacteria: N 2 0 + 2H' + 2e-N2 + H 2 0 .

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

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A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

Antholine

Kastrau

Steffens

et al. 1992

European Journal of Biochemistry

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185

170

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“…These studies were followed by the study of Jin et al [48], who studied the copper centers in N 2 OR by electron spin echo spectroscopy and presented further evidence for the similarity between the CuA center in the two enzymes. This similarity was also shown by magnetic circular dichroism (MCD) [49,50] and extended X-ray absorption fine structure (EXAFS) studies, as the curve-fitted copper EXAFS results for N 2 OR are strikingly similar to those for COX [50][51][52].…”

Section: The History Of the Cuz Centermentioning

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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“…protein by the method of Lowry et al [8]. The preparation used for experiments reported here had an initial protein concentration of 602 PM and 3.32 Cu per subunit.…”

Section: Febs Lettersmentioning

confidence: 99%

A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri)

Farrar¹,

Thomson²,

Cheesman³

et al. 1991

FEBS Letters

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117

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Nitrous oxide reductase (N2OR), Pseudomonas stutzeri, catalyses the 2 electron reduction of nitrous oxide to di‐nitrogen. The enzyme has 2 identical subunits (M 1 ∼ 70 000) of known amino acid sequence and contains ∼ 4 Cu ions per subunit. By measurement of the optical absorption, electron paramagnetic resonance (EPR) and low‐temperature magnetic circular dichroism (MCD) spectra of the oxidised state, a semi‐reduced form and the fully reduced state of the enzyme it is shown that the enzyme contains 2 distinct copper centres of which one is assigned to an electron‐transfer function, centre A, and the other to a catalytic site, centre Z. The latter is a binuclear copper centre with at least 1 cysteine ligand and cycles between oxidation levels Cu(II)/Cu(II) and Cu(II)/Cu(I) in the absence of substrate or inhibitors. The state Cu(II)/Cu(I) is enzymatically inactive. The MCD spectra provide evidence for a second form of centre Z, which may be enzymatically active, in the oxidised state of the enzyme. Centre A is structurally similar to that of CuA in bovine and bacterial cytochrome c oxidase and also contains copper ligated by cysteine. This centre may also be a binuclear copper complex.

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Copper coordination in nitrous oxide reductase from Pseudomonas stutzeri

Cited by 53 publications

References 0 publications

A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

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

A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri)

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