N2O Reduction by the μ4‐Sulfide‐Bridged Tetranuclear CuZ Cluster Active Site

Chen, Peng; Gorelsky, Serge I.; Ghosh, Santanu; Solomon, Edward I.

doi:10.1002/anie.200301734

Cited by 117 publications

(90 citation statements)

References 41 publications

(59 reference statements)

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“…The DFT calculations proposed that the substrate binds between two copper ions through a single oxygen atom. Although this model differs from the one of Solomon and coworkers, mentioned before, it is proposed to have similar activation energy [59].…”

Section: Catalytic Properties Of Cuz and Reaction Intermediatesmentioning

confidence: 70%

“…Cu I charge-transfer transition [59,70]. In particular, the three main frequency lines in the resonance Raman spectra, at 366, 386 and 415 cm -1 , are associated with Cu-S vibrations and contribute to the broad charge-transfer absorption band at approximately 640 nm (approximately 15,650 cm -1 ).…”

Section: Spectroscopy Of the Different Redox States Of The Cuz Centermentioning

confidence: 98%

“…The structure of the CuZ center opened a new chapter in the area of biological metal clusters, giving a structural basis for the interpretation of the spectroscopic data, and also providing the possibility to analyze these data using theoretical calculations [59].…”

Section: The History Of the Cuz Centermentioning

confidence: 99%

“…In those dithionite-reduced N 2 OR forms, the CuZ center is in the CuZ state (Table 1, form C) and the CuZ* state (Table 1, form-E), respectively. Dithionite-reduced CuZ and CuZ* are characterized by a broad absorption band with a maximum at around 640 nm and an EPR signal, with g values at 2.15-2.18 and 2.04-2.06 and four-line hyperfine splitting [28,59,67] (Table 2).…”

Section: Spectroscopy Of the Different Redox States Of The Cuz Centermentioning

confidence: 99%

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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: Catalytic Properties Of Cuz and Reaction Intermediatesmentioning

confidence: 70%

Section: Spectroscopy Of the Different Redox States Of The Cuz Centermentioning

confidence: 98%

Section: The History Of the Cuz Centermentioning

confidence: 99%

Section: Spectroscopy Of the Different Redox States Of The Cuz Centermentioning

confidence: 99%

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

et al. 2011

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“…nautica N 2 OR, in the as-isolated state, contains a 1Cu II /3Cu I redox state with a total spin of , where the unpaired electron is delocalized between two or more copper atoms through the bridging sulfide ion [10][11][12]. This state, which has a typical electronic spectral band at 640 nm and a four-line splitting EPR signature [13,14], cannot be easily reduced or oxidized.…”

Section: Introductionmentioning

confidence: 99%

A new CuZ active form in the catalytic reduction of N2O by nitrous oxide reductase from Pseudomonas nautica

et al. 2010

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The final step of bacterial denitrification, the two-electron reduction of N 2 O to N 2 , is catalyzed by a multicopper enzyme named nitrous oxide reductase. The catalytic centre of this enzyme is a tetranuclear copper site called CuZ, unique in biological systems. The in vitro reconstruction of the activity requires a slow activation in the presence of the artificial electron donor, reduced methyl viologen, necessary to reduce CuZ from the resting nonactive state (1Cu II /3Cu I ) to the fully reduced state (4Cu I ), in contrast to the turnover cycle, which is very fast. In the present work, the direct reaction of the activated form of Pseudomonas nautica nitrous oxide reductase with stoichiometric amounts of N 2 O allowed the identification of a new reactive intermediate of the catalytic centre, CuZ°, in the turnover cycle, characterized by an intense absorption band at 680 nm. Moreover, the first mediated electrochemical study of Ps. nautica nitrous oxide reductase with its physiological electron donor, cytochrome c-552, was performed. The intermolecular electron transfer was analysed by cyclic voltammetry, under catalytic conditions, and a second-order rate constant of (5.5 ± 0.9) 9 10 5 M -1 s -1 was determined. Both the reaction of stoichiometric amounts of substrate and the electrochemical studies show that the active CuZ°species, generated in the absence of reductants, can rearrange to the resting non-active CuZ state. In this light, new aspects of the catalytic and activation/inactivation mechanism of the enzyme are discussed.

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Nitrous Oxide Reductase

Eady

Antonyuk

Hasnain

2004

Handbook of Metalloproteins

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(N 2 O) is a major greenhouse gas and is thought to be some 300 times more potent than CO 2 in promoting global warming due to its inert chemical nature. The difficult chemistry of N 2 O reduction to gaseous nitrogen (N 2 ) in biology is catalyzed by the novel µ 4 ‐sulfide‐bridged tetranuclear Cu z cluster of the N 2 O reductases (N 2 ORs). These enzymes, in common with cytochrome c oxidase (CCO), also contain an electron‐donating Cu A site. During the past five years, several structures of this enzyme, from a number of species, have emerged, providing the details of structural elements responsible for this fascinating chemistry. These aspects are discussed in the light of extensive spectroscopic and functional data, providing an up‐to‐date review from these perspectives.

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N₂O Reduction by the μ₄‐Sulfide‐Bridged Tetranuclear Cu_Z Cluster Active Site

Cited by 117 publications

References 41 publications

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

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

A new CuZ active form in the catalytic reduction of N2O by nitrous oxide reductase from Pseudomonas nautica

Nitrous Oxide Reductase

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