Purification and characterization of the periplasmic nitrate reductase from <i>Thiosphaera pantotropha</i>

Berks, Ben C.; Richardson, David J.; Robinson, Carol; Reilly, Ann; Aplin, Robin T.; Ferguson, Stuart J.

doi:10.1111/j.1432-1033.1994.tb18605.x

Cited by 115 publications

(128 citation statements)

References 45 publications

(44 reference statements)

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“…The active site is a Mo bis(molybdopterin guanosine dinucleotide) (MobisMGD) cofactor and, in addition, there is a [4Fe-4S] cluster, likely involved in the electron transfer. Rs NapAB [21] and Pp NapAB [22] are heterodimeric proteins, but with their catalytic subunits closely related to Dd NapA. The structures of the catalytic subunits of Dd NapA [20] and Rs NapA [23] are very similar in terms of metal cofactor content, global fold, and domain organization.…”

Section: Introductionmentioning

confidence: 99%

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

et al. 2006

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Nitrate reductases are enzymes that catalyze the conversion of nitrate to nitrite. We report here electron paramagnetic resonance (EPR) studies in the periplasmic nitrate reductase isolated from the sulfatereducing bacteria Desulfovibrio desulfuricans ATCC 27774. This protein, belonging to the dimethyl sulfoxide reductase family of mononuclear Mo-containing enzymes, comprises a single 80-kDa subunit and contains a Mo bis(molybdopterin guanosine dinucleotide) cofactor and a [4Fe-4S] cluster. EPR-monitored redox titrations, carried out with and without nitrate in the potential range from 200 to À500 mV, and EPR studies of the enzyme, in both catalytic and inhibited conditions, reveal distinct types of Mo(V) EPR-active species, which indicates that the Mo site presents high coordination flexibility. These studies show that nitrate modulates the redox properties of the Mo active site, but not those of the [4Fe-4S] center. The possible structures and the role in catalysis of the distinct Mo(V) species detected by EPR are discussed.

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Section: Introductionmentioning

confidence: 99%

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

et al. 2006

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“…Apart from the membrane-bound nitrate reductase, also a periplasmic respiratory enzyme has been characterized in different denitrifying organisms including P. denitrificans and the closely related species Thiosphaera pantotropha (Bell et al, 1990;Berks et al, 1994;Sears et al, 1993). The latter enzyme is soluble and appears to consist of two subunits, one with a c-type heine and one with a molybdenum center (Breton et al, 1994).…”

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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“…Selenate reductase is dissimilar to the periplasmic nitrate reductases that have been purified from Rhodobacter sphaeroides, Alcaligenes eutrophus, and Thiosphaera pantotropha (3,(25)(26)(27). These enzymes consist of two subunits containing molybdopterin, possibly one [Fe-S] center and cytochrome c as prosthetic groups.…”

Section: Determination Of the N-terminal Amino Acid Sequence Of The Smentioning

confidence: 99%

Purification and Characterization of the Selenate Reductase from Thauera selenatis

Schröder¹,

Rech²,

Krafft³

et al. 1997

Journal of Biological Chemistry

215

183

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Thauera selenatis is one of two isolated bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The reduction of selenate to selenite is catalyzed by a selenate reductase, previously shown to be located in the periplasmic space of the cell. This study describes the purification of the enzyme from T. selenatis grown anaerobically with selenate. The enzyme is a trimeric ␣␤␥ complex with an apparent M r of 180,000. The ␣, ␤, and ␥ subunits are 96 kDa, 40 kDa, and 23 kDa, respectively, in size. The selenate reductase contains molybdenum, iron, and acid-labile sulfur as prosthetic group constituents. UV-visible absorption spectroscopy also revealed the presence of one cytochrome b per ␣␤␥ complex. The K m for selenate was determined to be 16 M, and the V max was 40 mol/min/mg of protein. The enzyme is specific for the reduction of selenate; nitrate, nitrite, chlorate, and sulfate were not reduced at detectable rates. These studies constitute the first description of a selenate reductase, which represents a new class of enzymes. The significance of this enzyme in relation to cell growth and energy generation is discussed.

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Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha

Cited by 115 publications

References 45 publications

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Purification and Characterization of the Selenate Reductase from Thauera selenatis

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