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- Pseudomonas aeruginosa MdaB and WrbA are Water-soluble Two-electron Quinone Oxidoreductases with the Potential to Defend against Oxidative Stress
- Laura K Green , Anne C La Flamme , David F Ackerley
- J. Microbiol. 2014;52(9):771-777. Published online August 2, 2014
- DOI: https://doi.org/10.1007/s12275-014-4208-8
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- 18 Crossref
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Abstract
- Water-soluble quinone oxidoreductases capable of reducing quinone substrates via a concerted two-electron mechanism have been implicated in bacterial antioxidant defence. Twoelectron transfer avoids formation of dangerously reactive semi-quinone intermediates, moreover previous work in Pseudomonas putida indicated a direct protective effect for the quinols generated by an over-expressed oxidoreductase. Here, the Pseudomonas aeruginosa orthologs of five quinone oxidoreductases – MdaB, ChrR, WrbA, NfsB, and NQO1 – were tested for their possible role in defending P. aeruginosa against H2O2 challenge. In in vitro assays, each enzyme was shown to reduce quinone substrates with only minimal semiquinone formation. However, when each was individually over-expressed in P. aeruginosa no overt H2O2-protective phenotype was observed. It was shown that this was due to a masking effect of the P. aeruginosa catalase, KatA; in a katA mutant, H2O2 challenged strains over-expressing the WrbA and MdaB orthologs grew significantly better than the empty plasmid control. A growth advantage was also observed for H2O2 challenged P. putida strains over-expressing P. aeruginosa wrbA, mdaB or katA. Despite not conferring a growth advantage to wild type P. aeruginosa, it is possible that these quinone oxidoreductases defend against H2O2 toxicity at lower concentrations.
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- Cyclic Isothiocyanate Goitrin Impairs Lotus japonicus Nodulation, Affects the Proteomes of Nodules and Free Mesorhizobium loti, and Induces the Formation of Caffeic Acid Derivatives in Bacterial Cultures
Seungwoo Jeong, Vadim Schütz, Fatih Demir, Matthias Preusche, Pitter Huesgen, Laurent Bigler, Filip Kovacic, Katharina Gutbrod, Peter Dörmann, Margot Schulz
Plants.2024; 13(20): 2897. CrossRef - Effects of the Quinone Oxidoreductase WrbA on Escherichia coli Biofilm Formation and Oxidative Stress
Federico Rossi, Cristina Cattò, Gianmarco Mugnai, Federica Villa, Fabio Forlani
Antioxidants.2021; 10(6): 919. CrossRef - Enrichment and description of novel bacteria performing syntrophic propionate oxidation at high ammonia level
Abhijeet Singh, Anna Schnürer, Maria Westerholm
Environmental Microbiology.2021; 23(3): 1620. CrossRef - Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi
Carla E. Lanze, Rafael M. Gandra, Jenna E. Foderaro, Kara A. Swenson, Lois M. Douglas, James B. Konopka
Microbiology and Molecular Biology Reviews.2020;[Epub] CrossRef - Diazaquinomycin Biosynthetic Gene Clusters from Marine and Freshwater Actinomycetes
Jana Braesel, Jung-Ho Lee, Benoit Arnould, Brian T. Murphy, Alessandra S. Eustáquio
Journal of Natural Products.2019; 82(4): 937. CrossRef - Kinetic Investigation of a Presumed Nitronate Monooxygenase from Pseudomonas aeruginosa PAO1 Establishes a New Class of NAD(P)H:Quinone Reductases
Renata A. G. Reis, Francesca Salvi, Isabella Williams, Giovanni Gadda
Biochemistry.2019; 58(22): 2594. CrossRef - Quantitative Proteomics of the 2016 WHO Neisseria gonorrhoeae Reference Strains Surveys Vaccine Candidates and Antimicrobial Resistance Determinants
Fadi E. El-Rami, Ryszard A. Zielke, Teodora Wi, Aleksandra E. Sikora, Magnus Unemo
Molecular & Cellular Proteomics.2019; 18(1): 127. CrossRef - Escherichia coli Modulator of Drug Activity B (MdaB) Has Different Enzymological Properties to Eukaryote Quinone Oxidoreductases
Clare F. Megarity, David J. Timson
Helvetica Chimica Acta.2019;[Epub] CrossRef - Identification of a Small Molecule Anti-biofilm Agent Against Salmonella enterica
Jasmine Moshiri, Darpan Kaur, Chido M. Hambira, Jenna L. Sandala, Jacob A. Koopman, James R. Fuchs, John S. Gunn
Frontiers in Microbiology.2018;[Epub] CrossRef - Kinetic Characterization of PA1225 from Pseudomonas aeruginosa PAO1 Reveals a New NADPH:Quinone Reductase
Elias Flores, Giovanni Gadda
Biochemistry.2018; 57(21): 3050. CrossRef - Pseudomonas aeruginosa ttcA encoding tRNA-thiolating protein requires an iron-sulfur cluster to participate in hydrogen peroxide-mediated stress protection and pathogenicity
Adisak Romsang, Jintana Duang-nkern, Khwannarin Khemsom, Lampet Wongsaroj, Kritsakorn Saninjuk, Mayuree Fuangthong, Paiboon Vattanaviboon, Skorn Mongkolsuk
Scientific Reports.2018;[Epub] CrossRef - WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System
Julien Herrou, Daniel M. Czyż, Jonathan W. Willett, Hye-Sook Kim, Gekleng Chhor, Gyorgy Babnigg, Youngchang Kim, Sean Crosson, A. M. Stock
Journal of Bacteriology.2016; 198(8): 1281. CrossRef - Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa
Vincenzo Crescente, Sinead M. Holland, Sapna Kashyap, Elena Polycarpou, Edith Sim, Ali Ryan
Biochemical Journal.2016; 473(5): 549. CrossRef - Functional Annotation of a Presumed Nitronate Monoxygenase Reveals a New Class of NADH:Quinone Reductases
Jacob Ball, Francesca Salvi, Giovanni Gadda
Journal of Biological Chemistry.2016; 291(40): 21160. CrossRef - Nitroreductase gene-directed enzyme prodrug therapy: insights and advances toward clinical utility
Elsie M. Williams, Rory F. Little, Alexandra M. Mowday, Michelle H. Rich, Jasmine V.E. Chan-Hyams, Janine N. Copp, Jeff B. Smaill, Adam V. Patterson, David F. Ackerley
Biochemical Journal.2015; 471(2): 131. CrossRef - The effects of indoor and outdoor dust exposure on the growth, sensitivity to oxidative-stress, and biofilm production of three opportunistic bacterial pathogens
Mohammed O. Suraju, Sloan Lalinde-Barnes, Sachindra Sanamvenkata, Mahsa Esmaeili, Shishir Shishodia, Jason A. Rosenzweig
Science of The Total Environment.2015; 538: 949. CrossRef - Flavodoxin-Like Proteins Protect Candida albicans from Oxidative Stress and Promote Virulence
Lifang Li, Shamoon Naseem, Sahil Sharma, James B. Konopka, Joachim Morschhäuser
PLOS Pathogens.2015; 11(9): e1005147. CrossRef - A novel cytosolic NADH:quinone oxidoreductase from Methanothermobacter marburgensis
Eva Ullmann, Tien Chye Tan, Thomas Gundinger, Christoph Herwig, Christina Divne, Oliver Spadiut
Bioscience Reports.2014;[Epub] CrossRef
- Cyclic Isothiocyanate Goitrin Impairs Lotus japonicus Nodulation, Affects the Proteomes of Nodules and Free Mesorhizobium loti, and Induces the Formation of Caffeic Acid Derivatives in Bacterial Cultures
- Metagenomic Assessment of a Sulfur-Oxidizing Enrichment Culture Derived from Marine Sediment
- Man-Young Jung , VinhHoa Pham , Soo-Je Park , So-Jeong Kim , Jong-Chan Chae , Yul Roh , Sung-Keun Rhee
- J. Microbiol. 2010;48(6):739-747. Published online January 9, 2011
- DOI: https://doi.org/10.1007/s12275-010-0257-9
- 44 View
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- 3 Scopus
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Abstract
- The biological oxidation of reduced sulfur compounds is a critically important process in global sulfur biogeochemistry. In this study, we enriched from marine sediments under denitrifying conditions, chemolithotrophic sulfur oxidizers that could oxidize a variety of reduced sulfur compounds: thiosulfate, tetrathionate, sulfide, and polysulfide. Two major phylotypes of 16S rRNA gene (>99% identity in each phylotype) were detected in this enrichment culture. In order to characterize sulfide oxidation, we sequenced and characterized one fosmid clone (43.6 kb) containing the group I sulfide-quinone reductase (sqr) gene. Interestingly, four putative rhodanese genes were found in this clone. Furthermore, comparative alignment with the closest genome of Thiomicrospira crunogena XCL2 revealed that three homologous genes were located within the vicinity of the sqr gene. Fosmid clones harboring carbon fixation (cbbL and cbbM) and denitrification (narG) genes were screened, and the phylogeny of the functional genes was analyzed. Along with the comparison between the sqr-containing fosmid clones and the relevant gamma-proteobacteria, our phylogenetic study based on the 16S rRNA gene and carbon fixation genes suggest the prevalence of chemolithotrophic gamma-proteobacteria in the denitrifying cultures. The findings of this study imply that a combination of cultivation and metagenomic approaches might provide us with a glimpse into the characteristics of sulfur oxidizers in marine sediments.
- Purification and Characterization of an Intracellular NADH: Quinone Reductase from Trametes versicolor
- Sang-Soo Lee , Dong-Soo Moon , Hyoung T. Choi , Hong-Gyu Song
- J. Microbiol. 2007;45(4):333-338.
- DOI: https://doi.org/2564 [pii]
- 49 View
- 0 Download
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Abstract
- Intracellular NADH:quinone reductase involved in degradation of aromatic compounds including lignin was purified and characterized from white rot fungus Trametes versicolor. The activity of quinone reductase was maximal after 3 days of incubation in fungal culture, and the enzyme was purified to homogeneity using ion-exchange, hydrophobic interaction, and gel filtration chromatographies. The purified enzyme has a molecular mass of 41 kDa as determined by SDS-PAGE, and exhibits a broad temperature optimum between 20-40°C, with a pH optimum of 6.0. The enzyme preferred FAD as a cofactor and NADH rather than NADPH as an electron donor. Among quinone compounds tested as substrate, menadione showed the highest enzyme activity followed by 1,4-benzoquinone. The enzyme activity was inhibited by CuSO4, HgCl2, MgSO4, MnSO4, AgNO3, dicumarol, KCN, NaN3, and EDTA. Its Km and Vmax with NADH as an electron donor were 23 μM and 101 mM/mg per min, respectively, and showed a high substrate affinity. Purified quinone reductase could reduce 1,4-benzoquinone to hydroquinone, and induction of this enzyme was higher by 1,4-benzoquinone than those of other quinone compounds.
- An FMN-containing NADH-quinone reductase from streptomyces sp
- Youn, Hong Duk , Lee, Jin Won , Youn, Hwan , Lee, Jeong Kug , Hah, Yung Chil , Kang, Sa Ouk
- J. Microbiol. 1996;34(2):206-213.
- 34 View
- 0 Download
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Abstract
- NADH-quinone reductase was purified 22-fold from the cytosolic fraction of Streptomyces sp. Imsnu-1 to apparent hemogenity, with an overall yield of 9%, by the purification procedure consisting of ammonium, sulfate precipitation and DEAE Sephacryl S-200 and DEAE 5 PW chromatographies. The molecular mass of the enzyme determined by gel filtration chromatography was found to be 110 kDa. SDS-PAGE revealed that the enzyme consists of two sugunits with a molecular mass of 54 kDa. The enzyme contained 1 mol of FMN per subunit as a cofactor. The A_272/A_457 ratio was 6.14 and the molar extinction coefficients were calculated to be 20, 800 and 25, 400M/sup -1/cm/sup -1/ AT 349 AND 457 nm, respectively. The N-terminal sequence of the enzyme contained the highly conserved fingerprint of ADP-binding domain. The enzyme used NADH as an electron donor and various quinones as electron acceptors. Cytochrome c was practically inactive. Air-stable flavin semiquinone was produced by the addition of NADH to the enzyme. Also, naphthosemiquinone was detected in the reaction mixture containing the enzyme.
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