The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17

Moir, James; Wehrfritz, Josa Marie; Spiro, Stephen; Richardson, David J.

doi:10.1042/bj3190823

Cited by 53 publications

(23 citation statements)

References 15 publications

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“…However, in heterotrophs ammonia oxidation cannot support lithoautotrophic growth. One reason may be that oxidation of NH # OH by a periplasmic hydroxylamine oxidase requires oxygen rather than water (Moir et al, 1996 ;Richardson et al, 1998) and thus yields only two reducing equivalents. These can be transferred to either the nitrite reductase, nitrous oxide reductase or nitric oxide reductase, so that the nitrite produced can ultimately be reduced to N # (Fig.…”

Section: Multiple Physiological Roles For Normentioning

confidence: 99%

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

2000

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Section: Multiple Physiological Roles For Normentioning

confidence: 99%

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

2000

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“…The images on the right are rotated by 90°with respect to those on the left, so the proposed electron entry site is facing the reader. The images were prepared using the USCF Chimera program [35] b electrostatic character has also been suggested for other electron transfer complexes involving pseudoazurin and/or cytochrome c-550 from these organisms, and P. panthotropus cytochrome c peroxidase [48] and P. denitrificans non-heme-iron hydroxylamine oxidase [50].…”

Section: General Analysismentioning

confidence: 99%

The electron transfer complex between nitrous oxide reductase and its electron donors

Dell’Acqua

Moura

et al. 2011

J Biol Inorg Chem

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Identifying redox partners and the interaction surfaces is crucial for fully understanding electron flow in a respiratory chain. In this study, we focused on the interaction of nitrous oxide reductase (N 2 OR), which catalyzes the final step in bacterial denitrification, with its physiological electron donor, either a c-type cytochrome or a type 1 copper protein. The comparison between the interaction of N 2 OR from three different microorganisms, Pseudomonas nautica, Paracoccus denitrificans, and Achromobacter cycloclastes, with their physiological electron donors was performed through the analysis of the primary sequence alignment, electrostatic surface, and molecular docking simulations, using the bimolecular complex generation with global evaluation and ranking algorithm. The docking results were analyzed taking into account the experimental data, since the interaction is suggested to have either a hydrophobic nature, in the case of P. nautica N 2 OR, or an electrostatic nature, in the case of P. denitrificans N 2 OR and A. cycloclastes N 2 OR. A set of well-conserved residues on the N 2 OR surface were identified as being part of the electron transfer pathway from the redox partner to N 2 OR (Ala495, Asp519, Val524, His566 and Leu568 numbered according to the P. nautica N 2 OR sequence). Moreover, we built a model for Wolinella succinogenes N 2 OR, an enzyme that has an additional c-type-heme-containing domain. The structures of the N 2 OR domain and the c-type-heme-containing domain were modeled and the full-length structure was obtained by molecular docking simulation of these two domains. The orientation of the c-type-heme-containing domain relative to the N 2 OR domain is similar to that found in the other electron transfer complexes.

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“…It has been reported that HAOs are distinct from different organisms. HAO from P. denitrificans is a small periplasmic monomer (20-kDa) containing ferric iron [21], while the enzyme from Pseudomonas PB16 is a homo-dimer of 68-kDa subunits with no detectable cofactors [22]. In the present study, hydroxylamine oxidoreductase gene was not identified.…”

Section: Resultsmentioning

confidence: 42%

Draft Genome Sequence of Acinetobacter Y1, a Heterotrophic Nitrifying and Aerobic Denitrifying Bacterium Isolated from Coke Plant Wastewater

Yang¹,

Yang²,

Liu³

et al. 2017

Proceedings of the 2nd 2016 International Conference on Sustainable Development (ICSD 2016)

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Abstract-Acinetobacter sp. Y1, with a remarkable capability of heterotrophic nitrification and aerobic denitrification, was isolated from the activated sludge of a coke plant wastewater. It can simultaneously remove specific organic matter and different nitrogen (ammonium nitrogen, nitrite nitrogen and nitrate nitrogen). For further study of the mechanism of nitrogen removal, its draft genome was sequenced. Results show that the 3, 384, 069 bp draft genome consists of 24 scaffolds with 3173 protein-coding sequences, 63 tRNAs and 8 rRNAs. Of the total protein-coding sequences, 99.15% had hits in the NR database. KEGG database annotation results indicate 1708 genes involved in 167 metabolic pathways and possessed the genes of degrading many types of organic chemicals. Multiple genes relating to nitrogen metabolism and degrading many types of organic chemicals were annotated.

show abstract

The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17

Cited by 53 publications

References 15 publications

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

The electron transfer complex between nitrous oxide reductase and its electron donors

Draft Genome Sequence of Acinetobacter Y1, a Heterotrophic Nitrifying and Aerobic Denitrifying Bacterium Isolated from Coke Plant Wastewater

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