Copper Protein Structures

Adman, Elinor T.

doi:10.1016/s0065-3233(08)60536-7

Cited by 596 publications

(584 citation statements)

References 114 publications

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“…Two types of nitrite reductase have been identified in denitrifying bacteria: (i) a homo-dimer with c and dl type hemes (Fig. 3A) (Stouthamer, 1991), and (ii) a homo-trimer with two distinct copper centers (not shown) (Adman, 1991). P. denitrificans possesses the cdl type nitrate reductase (Fig.…”

Section: The Anaerobic Respiratory Networkmentioning

confidence: 99%

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Spanning

Boer

Reijnders

et al. 1995

J Bioenerg Biomembr

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General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018Journal of Bioenergetics and Biomembranes, Vol. 27, No. 5, 1995 Received May 29, 1995 Paracoccus denitrificans is a facultative anaerobic bacterium that has the capacity to adjust its metabolic infrastructure, quantitatively and/or qualitatively, to the prevailing growth condition. In this bacterium the relative activity of distinct catabolic pathways is subject to a hierarchical control. In the presence of oxygen the aerobic respiration, the most efficient way of electron transfer-linked phosphorylation, has priority. At high oxygen tensions P. denitrificans synthesizes an oxidase with a relatively low affinity for oxygen, whereas under oxygen limitation a high-affinity oxidase appears specifically induced. During anaerobiosis, the pathways with lower free energy-transducing efficiency are induced. In the presence of nitrate, the expression of a number of dehydrogenases ensures the continuation of oxidative pbosphorylation via denitrification. After identification of the structural components that are involved in both the aerobic and the anaerobic respiratory networks of P. denitrificans, the intriguing next challenge is to get insight in its regulation. Two transcription regulators have recently been demonstrated to be involved in the expression of a number of aerobic and/or anaerobic respiratory complexes in P. denitrificans. Understanding of the regulation machinery is beginning to emerge and promises much excitement in discovery.KEY WORDS: Respiratory network; multiple oxidases; denitrification; gene regulation; FNR; Paracoccus denitrificans; Escherichia coli. ~TRODUCTIONThe ultimate goal of living organisms is to contribute to a continued existence of their species by means of survival and reproduction. In unicellular organisms, the ability to survive depends on the cell's potential to adapt its metabolism to the available carbon and free-energy sources in its natural habitat, ensuring maintenance and growth. The more such an environment is subject to fluctuations in the supply of these substrates, the higher the demands that are made upon the potential of the cell to adjust its metabolic properties. A profound example of this flexibility is the process of bacterial respiration...

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Section: The Anaerobic Respiratory Networkmentioning

confidence: 99%

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Spanning

Boer

Reijnders

et al. 1995

J Bioenerg Biomembr

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“…Most of the copper centers present in these proteins can be divided into three classes (type 1, type 2, and type 3) [17][18][19]. However, recently new protein structures and spectroscopic data have led to the identification of two novel copper sites that cannot be classified into the initial division.…”

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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“…Stellacyanin (St hereafter) is a glycoprotein isolated from the lacquer tree Rhus verniczjha [5,6], which has been considered an outlier in the family of BCPs due to its unusually low redox potential [6], high electron transfer rates [7] and its spectroscopic features. All BCPs contain a so-called type 1 copper center, in which the metal ion lies in a plane defined by three ligands: two histidines and one cysteine [2]. A methionine residue is one axial ligand, and a glycine backbone carbonyl has been found coordinated to the copper in azurin at a longer distance [2].…”

Section: Introductionmentioning

confidence: 99%

A ¹H NMR NOE study on Co(II) stellacyanin: Some clues about the structure of the metal site

Vila

1994

FEBS Letters

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The 'H NMR spectrum of Co(H) stellacyanin is reported, in which four signals not previously observed have been detected. NOE experiments were performed to assign the hyperfine shifted signals corresponding to a Cys and two His residues. Both His residues are solventaccessible and are shown to bind the metal ion through their NJ1 atoms. The j?-CH, Cys proton shifts indicate the presence of a strong axial ligand.

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Copper Protein Structures

Cited by 596 publications

References 114 publications

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

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

A ¹H NMR NOE study on Co(II) stellacyanin: Some clues about the structure of the metal site

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Copper Protein Structures

Cited by 596 publications

References 114 publications

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

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

A 1H NMR NOE study on Co(II) stellacyanin: Some clues about the structure of the metal site

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A ¹H NMR NOE study on Co(II) stellacyanin: Some clues about the structure of the metal site