Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri

Heiss, Bernd; Frunzke, Kurt; Zumft, Walter G.

doi:10.1128/jb.171.6.3288-3297.1989

Cited by 176 publications

(161 citation statements)

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“…S3) (5,(12)(13)(14)(15)(16)(17)(18)(19)21). The recombinant TtcNOR has the same properties whether it is isolated from an E. coli or from a T. thermophilus expression system.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the nitric oxide reductase from Thermus thermophilus

Schurig-Briccio

Venkatakrishnan

Hemp

et al. 2013

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

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Nitrous oxide (N 2 O) is a powerful greenhouse gas implicated in climate change. The dominant source of atmospheric N 2 O is incomplete biological dentrification, and the enzymes responsible for the release of N 2 O are NO reductases. It was recently reported that ambient emissions of N 2 O from the Great Boiling Spring in the United States Great Basin are high, and attributed to incomplete denitrification by Thermus thermophilus and related bacterial species [Hedlund BP, et al. (2011) Geobiology 9(6)471–480]. In the present work, we have isolated and characterized the NO reductase (NOR) from T. thermophilus . The enzyme is a member of the cNOR family of enzymes and belongs to a phylogenetic clade that is distinct from previously examined cNORs. Like other characterized cNORs, the T. thermophilus cNOR consists of two subunits, NorB and NorC, and contains a one heme c , one Ca 2+ , a low-spin heme b , and an active site consisting of a high-spin heme b and Fe B . The roles of conserved residues within the cNOR family were investigated by site-directed mutagenesis. The most important and unexpected result is that the glutamic acid ligand to Fe B is not essential for function. The E211A mutant retains 68% of wild-type activity. Mutagenesis data and the pattern of conserved residues suggest that there is probably not a single pathway for proton delivery from the periplasm to the active site that is shared by all cNORs, and that there may be multiple pathways within the T. thermophilus cNOR.

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“…S3) (5,(12)(13)(14)(15)(16)(17)(18)(19)21). The recombinant TtcNOR has the same properties whether it is isolated from an E. coli or from a T. thermophilus expression system.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the nitric oxide reductase from Thermus thermophilus

Schurig-Briccio

Venkatakrishnan

Hemp

et al. 2013

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

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“…The third step in denitrification is the reduction of nitric oxide to nitrous oxide (2NO + 2H § + 2e-N20 + H20), catalyzed by the membrane-bound enzyme nitric oxide reductase (Nor) (Heiss et al, 1989;Carr and Ferguson, 1990;Zumft et al, 1994). Nor receives electrons via the bCl complex but it is not known which electron carriers, if any, mediate this transport.…”

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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“…In Enemark and Feltham formulism, 24 which counts metal d-electrons plus the lone π* electron from the nitrosyl ligand, iron(II)-NO and iron(III)-NO complexes are represented as {FeNO} 7 and {FeNO} 6 species, respectively. Crystal structures of metal-nitrosyl porphyrin complexes have shown that {MNO} 6 species adopt a linear M-N-O structure, while {MNO} 7 species have bent M-N-O configurations.…”

Section: Spectroscopic Signatures Of Heme Iron-nitrosyl Complexesmentioning

confidence: 99%

“…30,[50][51][52][53][54] The ν 3 and ν 10 porphyrin core modes are observed at higher frequencies in {FeNO} 6 than in 6-coordinate {FeNO} 7 species. 30,[50][51][52][53][54] Importantly, vibrational modes of the FeNO unit in {FeNO} 6 species do not seem to correlate with those of {FeNO} 7 and carbonyl complexes. In fact, ferric-nitrosyl complexes in P450cam, with various substrates bound in the distal pocket, reveal a direct correlation between ν(Fe-NO) and ν(NO) rather than the inverse correlation observed between ν(Fe-XO) and ν(X-O) (i.e., where X = N or C) in {FeNO} 7 and carbonyl complexes.…”

Section: Spectroscopic Signatures Of Heme Iron-nitrosyl Complexesmentioning

confidence: 99%

“…[4][5][6] Purification of NO reductases from a variety of denitrifying bacteria have confirmed that the NorB subunit (53 kDa) anchors one high-spin heme b 3 and one non-heme iron now known as Fe B , in analogy with Cu B in CcO. [5][6][7][8][9] Similar to the terminal oxidase superfamily, the NOR family exhibits variability in the electron-entry portion of the enzyme (Fig. 1).…”

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confidence: 99%

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Spectroscopic characterization of heme iron–nitrosyl species and their role in NO reductase mechanisms in diiron proteins

Moënne‐Loccoz

2007

Nat. Prod. Rep.

121

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Nitric oxide (NO) plays an important role in cell signalling and in the mammalian immune response to infection. On its own, NO is a relatively inert radical, and when it is used as a signalling molecule, its concentration remains within the picomolar range. However, at infection sites, the NO concentration can reach the micromolar range, and reactions with other radical species and transition metals lead to a broad toxicity. Under aerobic conditions, microorganisms cope with this nitrosative stress by oxidizing NO to nitrate (NO 3 − ). Microbial hemoglobins play an essential role in this NO-detoxifying process. Under anaerobic conditions, detoxification occurs via a 2-electron reduction of two NO molecules to N 2 O. In many bacteria and archaea, this NOreductase reaction is catalyzed by diiron proteins. Despite the importance of this reaction in providing microorganisms with a resistance to the mammalian immune response, its mechanism remains ill-defined. Because NO is an obligatory intermediate of the denitrification pathway, respiratory NO reductases also provide resistance to toxic concentrations of NO. This family of enzymes is the focus of this review. Respiratory NO reductases are integral membrane protein complexes that contain a norB subunit evolutionarily related to subunit I of cytochrome c oxidase (CcO). NorB anchors one high-spin heme b 3 and one non-heme iron known as Fe B , i.e., analogous to Cu B in CcO. A second group of diiron proteins with NO-reductase activity is comprised of the large family of soluble flavoprotein A found in strict and facultative anaerobic bacteria and archaea. These soluble detoxifying NO reductases contain a non-heme diiron cluster with a Fe-Fe distance of 3.4 Å and are only briefly mentioned here as a promising field of research. This article describes possible mechanisms of NO reduction to N 2 O in denitrifying NO-reductase (NOR) proteins and critically reviews recent experimental results. Relevant theoretical model calculations and spectroscopic studies of the NO-reductase reaction in heme/copper terminal oxidases are also overviewed.

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Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri

Cited by 176 publications

References 57 publications

Characterization of the nitric oxide reductase from Thermus thermophilus

Characterization of the nitric oxide reductase from Thermus thermophilus

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Spectroscopic characterization of heme iron–nitrosyl species and their role in NO reductase mechanisms in diiron proteins

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