Journal of Microbiology

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Paenibacillus nuruki sp. nov., isolated from Nuruk, a Korean fermentation starter: Soo-Jin Kim , Hayoung Cho , Jae-Hyung Ahn , Hang-Yeon Weon , Jae-Ho Joa , Jeong-Seon Kim , Soon-Wo Kwon; J. Microbiol. 2019;57(10):836-841. Published online June 27, 2019; DOI: https://doi.org/10.1007/s12275-019-9118-3

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A Gram-stain-positive, rod-shaped, non-endospore-forming, motile by means of peritrichous flagella, facultatively anaerobic bacterium designated TI45-13arT was isolated from Nuruk, a Korean traditional Makgeolli fermentation starter. It grew at 4–35°C (optimum, 28–30°C), pH 5.0–9.0 (optimum, pH 7.0) and NaCl concentrations up to 5% (w/v). Phylogenetic trees generated using 16S rRNA gene sequences revealed that strain TI45-13arT belonged to the genus Paenibacillus and showed the highest sequence similarities with Paenibacillus kyungheensis DCY88T (98.5%), Paenibacillus hordei RH-N24T (98.4%) and Paenibacillus nicotianae YIM h-19T (98.1%). The major fatty acid was anteiso-C15:0. The DNA G+C content was 39.0 mol%, and MK-7 was the predominant isoprenoid quinone. The polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylethanolamine, three unidentified glycolipids, and one unidentified aminoglycolipid. The cell-wall peptidoglycan contained meso-diaminopimelic acid. On the basis of polyphasic taxonomy study, it was suggested that strain TI45-13arT represents a novel species within the genus Paenibacillus for which the name Paenibacillus nuruki sp. nov. is proposed. The type strain was TI45-13arT (= KACC 18728T = NBRC 112013T).

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Paenibacillus dendrobii sp. nov., an indole-3-acetic acid-producing endophytic bacterium isolated from Dendrobium nobile
Yadong Hu, Hongjie Li, Yaoyi Chen, Qiling Zhang, Shigang Zheng, Dan Rao, Ze Chun, Ruoxi Zhao
International Journal of Systematic and Evolutionary Microbiology .2023;[Epub] CrossRef
Makgeolli - The Traditional Choice of Korean Fermented Beverage from Cereal: An Overview on its Composition and Health Benefits
Ganesh SHIMOGA, Sang-Youn KIM
Food Science and Technology.2022;[Epub] CrossRef
Integrative Metagenomics–Metabolomics for Analyzing the Relationship Between Microorganisms and Non-volatile Profiles of Traditional Xiaoqu
Chi Zhao, Wei Su, Yu Mu, Yingchun Mu, Li Jiang
Frontiers in Microbiology.2021;[Epub] CrossRef
Flaviflexus ciconiae sp. nov., isolated from the faeces of the oriental stork, Ciconia boyciana
Jae-Yun Lee, Woorim Kang, Pil Soo Kim, So-Yeon Lee, Na-Ri Shin, Hojun Sung, June-Young Lee, Ji-Hyun Yun, Yun-Seok Jeong, Jeong Eun Han, Mi-Ja Jung, Dong-Wook Hyun, Hyun Sik Kim, Euon Jung Tak, Jin-Woo Bae
International Journal of Systematic and Evolutionary Microbiology.2020; 70(10): 5439. CrossRef

The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT: Thinh-Phat Cao , Jin Myung Choi , Si Wouk Kim , Sung Haeng Lee; J. Microbiol. 2018;56(4):246-254. Published online February 28, 2018; DOI: https://doi.org/10.1007/s12275-018-7483-y

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Abstract

The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MPT (MDHMas), was determined at 1.7 Å resolution. The active form of MDHMas (or MDHIMas) is a heterotetrameric α2β2, where each β-subunit assembles on one side of each of the α-subunits, in a symmetrical fashion, so that two β-subunits surround the two PQQ-binding pockets on the α-subunits. The active site consists of a PQQ molecule surrounded by a β-propeller fold for each α-subunit. Interestingly, the PQQ molecules are coordinated by a Mg2+ ion, instead of the Ca2+ ion that is commonly found in the terrestrial MDHI, indicating the efficiency of osmotic balance regulation in the high salt environment. The overall interaction of the β-subunits with the α-subunits appears tighter than that of terrestrial homologues, suggesting the efficient maintenance of MDHIMas integrity in the sea water environment to provide a firm basis for complex formation with MxaJMas or Cyt cL. With the help of the features mentioned above, our research may enable the elucidation of the full molecular mechanism of methanol oxidation by taking advantage of marine bacterium-originated proteins in the methanol oxidizing system (mox), including MxaJ, as the attainment of these proteins from terrestrial bacteria for structural studies has not been successful.

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Computational insights into the molecular dynamics of the binding of ligands in the methanol dehydrogenase
One-Sun Lee, Sung Haeng Lee
Chemistry Letters.2024;[Epub] CrossRef
Formaldehyde: An Essential Intermediate for C1 Metabolism and Bioconversion
Mengshi Jia, Mengge Liu, Jiawen Li, Wankui Jiang, Fengxue Xin, Wenming Zhang, Yujia Jiang, Min Jiang
ACS Synthetic Biology.2024; 13(11): 3507. CrossRef
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Betina Cecilia Agaras, Cecilia Eugenia María Grossi, Rita María Ulloa
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Emily R. Featherston, Joseph A. Cotruvo
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Bioinorganic insights of the PQQ-dependent alcohol dehydrogenases
Pedro D. Sarmiento-Pavía, Martha E. Sosa-Torres
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Bioinformatic analysis of subfamily-specific regions in 3D-structures of homologs to study functional diversity and conformational plasticity in protein superfamilies
Daria Timonina, Yana Sharapova, Vytas Švedas, Dmitry Suplatov
Computational and Structural Biotechnology Journal.2021; 19: 1302. CrossRef
Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy
Thien-Kim Le, Yu-Jin Lee, Gui Hwan Han, Soo-Jin Yeom
Frontiers in Bioengineering and Biotechnology.2021;[Epub] CrossRef
Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function
Nathan M. Good, Matthias Fellner, Kemal Demirer, Jian Hu, Robert P. Hausinger, N. Cecilia Martinez-Gomez
Journal of Biological Chemistry.2020; 295(24): 8272. CrossRef
Zebra2: advanced and easy-to-use web-server for bioinformatic analysis of subfamily-specific and conserved positions in diverse protein superfamilies
Dmitry Suplatov, Yana Sharapova, Elizaveta Geraseva, Vytas Švedas
Nucleic Acids Research.2020; 48(W1): W65. CrossRef
Biological Pincer Complexes
Jorge L. Nevarez, Aiko Turmo, Jian Hu, Robert P. Hausinger
ChemCatChem.2020; 12(17): 4242. CrossRef
Crystal structure of Cytochrome cL from the aquatic methylotrophic bacterium Methylophaga aminisulfidivorans MPT
Suparna Ghosh, Immanuel Dhanasingh, Jaewon Ryu, Si Wouk Kim, Sung Haeng Lee
Journal of Microbiology and Biotechnology.2020; 30(8): 1261. CrossRef
New metal cofactors and recent metallocofactor insights
Robert P Hausinger
Current Opinion in Structural Biology.2019; 59: 1. CrossRef
Lanthanides‐based catalysis in eukaryotes
Giovanna De Simone, Fabio Polticelli, Silvio Aime, Paolo Ascenzi
IUBMB Life.2018; 70(11): 1067. CrossRef

Lysobacter tyrosinelyticus sp. nov. isolated from Gyeryongsan national park soil: Juan Du , Hina Singh , Hien T.T. Ngo , KyungHwa Won , Ki-Young Kim , Tae-Hoo Yi; J. Microbiol. 2015;53(6):365-370. Published online May 30, 2015; DOI: https://doi.org/10.1007/s12275-015-4729-9

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Abstract

A novel Gram-negative, rod-shaped (0.2-0.5 um x 1.5-2.5 um), aerobic, non-motile bacterium was isolated from Gyeryongsan national park soil, Republic of Korea. The novel isolate was designated as THG-DN8.2T. The strain grows optimally at 28oC, at pH 7 and in the absence of NaCl. Phylogenetic analysis based on 16S rRNA gene sequence showed that the novel isolate shared the highest sequence similarity with Lysobacter oryzae KCTC 22249T followed by Lysobacter yangpyeongensis KACC 11407T and Lysobacter niabensis KACC 11587T. The DNA G+C content of strain THG-DN8.2T is 66.0 mol% and ubiquinone Q-8 is the main isoprenoid quinone. The major polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylethanolamine, and phosphatidyl-N-methylethanolamine. The major fatty acids of strain THG-DN8.2T were identified as iso-C15:0, iso-C16:0, and C16:1w7c alcohol. The phylogenetic distinctiveness and phenotypic characteristics differentiated strain THG-DN8.2T from closely related Lysobacter species. The results of polyphasic taxonomic analysis suggest that strain THG-DN8.2T represents a novel species of the genus Lysobacter, for which the name Lysobacter tyrosinelyticus sp. nov. is proposed. The type strain is THG-DN8.2T (=KCTC 42235T =JCM 30320T).

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Lysobacter ciconiae sp. nov., and Lysobacter avium sp. nov., isolated from the faeces of an Oriental stork
So-Yeon Lee, Pil Soo Kim, Hojun Sung, Dong-Wook Hyun, Jin-Woo Bae
Journal of Microbiology.2022; 60(5): 469. CrossRef
Application of Bioorganic Fertilizer on Panax notoginseng Improves Plant Growth by Altering the Rhizosphere Microbiome Structure and Metabolism
Rui Shi, Shu Wang, Bingjie Xiong, Haiyan Gu, Huiling Wang, Chao Ji, Weijia Jia, Abraham Rami Horowitz, Wenjie Zhen, Jiftah Ben Asher, Xiahong He
Microorganisms.2022; 10(2): 275. CrossRef
Lysobacter arenosi sp. nov. and Lysobacter solisilvae sp. nov. isolated from soil
Kyeong Ryeol Kim, Kyung Hyun Kim, Shehzad Abid Khan, Hyung Min Kim, Dong Min Han, Che Ok Jeon
Journal of Microbiology.2021; 59(8): 709. CrossRef
Analysis of the Intestinal Flora in Male Versus Female Swamp Eels (Monopterus albus)
Ying Wang, Jinhua Zhang, Qiubai Zhou, Zirui Wang, Miao Gao, Xin Yang, Yu Liu, Zhengzhou Zhang, Wenhao Jiang, Chonghua Hu, Wenping Zhang
Frontiers in Microbiology.2020;[Epub] CrossRef
Lysobacter terricola sp. nov., isolated from greenhouse soil
Soo-Jin Kim, Jae-Hyung Ahn, Hang-Yeon Weon, Seung-Beom Hong, Soon-Ja Seok, Jeong-Seon Kim, Soon-Wo Kwon
International Journal of Systematic and Evolutionary Microbiology.2016; 66(3): 1401. CrossRef
Changes in the soil microbial community after reductive soil disinfestation and cucumber seedling cultivation
Xinqi Huang, Liangliang Liu, Teng Wen, Jinbo Zhang, Fenghe Wang, Zucong Cai
Applied Microbiology and Biotechnology.2016; 100(12): 5581. CrossRef
Diversity and Activity of Lysobacter Species from Disease Suppressive Soils
Ruth Gómez Expósito, Joeke Postma, Jos M. Raaijmakers, Irene De Bruijn
Frontiers in Microbiology.2015;[Epub] CrossRef

Research Support, Non-U.S. Gov'ts

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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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
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Jasmine Moshiri, Darpan Kaur, Chido M. Hambira, Jenna L. Sandala, Jacob A. Koopman, James R. Fuchs, John S. Gunn
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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
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Julien Herrou, Daniel M. Czyż, Jonathan W. Willett, Hye-Sook Kim, Gekleng Chhor, Gyorgy Babnigg, Youngchang Kim, Sean Crosson, A. M. Stock
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Vincenzo Crescente, Sinead M. Holland, Sapna Kashyap, Elena Polycarpou, Edith Sim, Ali Ryan
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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
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Mohammed O. Suraju, Sloan Lalinde-Barnes, Sachindra Sanamvenkata, Mahsa Esmaeili, Shishir Shishodia, Jason A. Rosenzweig
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Lifang Li, Shamoon Naseem, Sahil Sharma, James B. Konopka, Joachim Morschhäuser
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A novel cytosolic NADH:quinone oxidoreductase from Methanothermobacter marburgensis
Eva Ullmann, Tien Chye Tan, Thomas Gundinger, Christoph Herwig, Christina Divne, Oliver Spadiut
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NOTE] Characterization of a Mutant Strain of a Filamentous Fungus Cladosporium phlei for the Mass Production of the Secondary Metabolite Phleichrome: Min-Hee Yi , Jung-Ae Kim , Jung-Mi Kim , Jin-Ah Park , Beom-Tae Kim , Seung-Moon Park , Moon-Sik Yang , Ki-Jun Hwang , Dae-Hyuk Kim; J. Microbiol. 2011;49(4):680-683. Published online September 2, 2011; DOI: https://doi.org/10.1007/s12275-011-1022-4

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Abstract: UV-mutagenesis was performed to obtain mutant strains that demonstrate altered production of phleichrome, a secondary metabolite of Cladosporium phlei. Among fifty mutants selected, based on the increased area and intensity of the purple pigment surrounding the colonies, the strain M0035 showed the highest production of phleichrome, more than seven fold over wild type. Plate cultures of the M0035 strain resulted in a total of 592 mg phleichrome consisting of 146 mg and 446 mg from the mycelia and agar media, respectively. The M0035 strain displayed a growth rate and a mycelial mass comparable to the parental strain but had significantly reduced asexual sporulation.

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

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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.

Inactivation of Barotolerant Strains of Listeria monocytogenes and Escherichia coli O157:H7 by Ultra High Pressure and tert-Butylhydroquinone Combination: Yoon-Kyung Chung , Ahmed E. Yousef; J. Microbiol. 2008;46(3):289-294. Published online July 5, 2008; DOI: https://doi.org/10.1007/s12275-008-0090-6

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Abstract: Antimicrobial efficacy of ultra-high-pressure (UHP) can be enhanced by application of additional hurdles. The objective of this study was to systematically assess the enhancement in pressure lethality by TBHQ treatment, against barotolerant strains of Escherichia coli O157:H7 and Listeria monocytogenes. Two L. monocytogenes Scott A and the barotolerant OSY-328 strain, and two E. coli O157:H7 strains, EDL-933 and its barotolerant mutant, OSY-ASM, were tested. Cell suspensions containing TBHQ (50 ppm, dissolved in dimethyl sulfoxide) were pressurized at 200 to 500 MPa (23±2°C) for 1 min, plated on tryptose agar and enumerated the survivors. The TBHQ-UHP combination resulted in synergistic inactivation of both pathogens, with different degrees of lethality among strains. The pressure lethality threshold, for the combination treatment, was lower for E. coli O157:H7 (≥ 200 MPa) than for L. monocytogenes (> 300 MPa). E. coli O157:H7 strains were extremely sensitive to the TBHQ-UHP treatment, compared to Listeria strains. Interestingly, a control treatment involving DMSO-UHP combination consistently resulted in higher inactivation than that achieved by UHP alone, against all strains tested. However, sensitization of the pathogens to UHP by the additives (TBHQ in DMSO) was prominently greater for UHP than DMSO. Differences in sensitivities to the treatment between these two pathogens may be attributed to discrepancies in cellular structure or physiological functions.

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]

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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.

Lipid analysis of streptomycetes isolated form volcanic soil: Kim, Seung Bum , Kim, Min Young , Seong, Chi Nam , Kang Sa Ouk , Hah, Yung Chil; J. Microbiol. 1996;34(2):184-191.

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Abstract: The cellular fatty acids and quinones of streptomycetes isolated from volcanic soils were analysed. The strains contained fatty acids of 14 to 17 carbon chains, and 12-methyltetradecanoic acid and 14 methylpentadecanoic acid were dominant in most strains. The total profiles consisted of 74% branched fatty acid family, 16.8% linear family and 8.2% unsaturated family. The largest cluster of grey spore masses defined by numerical classification was separated from the remainders in the principal component analysis, but the other clusters were overlapped with one another. In the analysis of respiratory quinones, all of the strains contained either the menaquinone of 9 isoprene units with 6 hydrogenations of 8 hydrogenations as the major species. The distribution of menaquinones among the clusters could provide an important key in the chemotaxonomy of streptomycetes.

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.

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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.

Kinetic and spectral investigations on Ca^2+ and Sr^2+ containing methanol dehydrogenases: Kim, Si Wouk , Kim, Chung, Sung , Lee, Jung Sup , Koh, Moon Joo , Yang, Song Suk , Duine, Johannis A. , Kim, Young Min; J. Microbiol. 1997;35(3):200-205.

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Abstract: Both Ca^2+ and Sr^2+ containing methanol dehydrogenases (MDH) were purified to homogeneity with yields of 48% and 42%, respectively, from Methylabacillus methanolovorus sp. strain SK5. Most of the biochemical and structural properties were similar to each other. However, some differences were found: (1) although the overall shape of the absorption spectrum of Sr^2+ MDH was very similar to that of Ca^2+ MDH, the absorption intensity originating from the cofactor in Sr^2+. MDH was higher than that in Ca^2+-MDH. Small blue shift of the maximum was also observed. These are probably due to a difference in redox state of the cofactors in Ca^2+ and Sr^2+ -MDH; (2)Sr^2+ -MDH was more heat-stable than Ca^2+-MDH above 56℃; (3) the V_max values for the methanol-dependent activities of Sr^2+ Ca^2+ -MDH in the presence of 3 mM KCN were 2.038 and 808 nmol/mg protein/min, respectively. In addition, the K_m values of Sr^2+ and Ca^2+ MDH for methanol were 12 and 21 uM, respectively; (4) the endogenous activity of Ca^2+ -MDH was more sensitive than that of Sr^2+ -MDH in the presence of cyanide; (5) Diethyl pyrocarbonate treatment increased the enzyme activities of Ca^2+ and Sr^2+ MDH 4.2 and 1.4 folds, respectively. These results indicate that Sr^2+ stabilizes the structural conformation and enhances the activity of MDH more than Ca^2+.

Glutathione Content and the Activities of GlutathioneSynthesizing Enzymes in Fission Yeast are Modulated by Oxidative Stress: Yuk-Young Lee , Su-Jung Kim , Eun-Hee Park , Chang-Jin Lim; J. Microbiol. 2003;41(3):248-251.

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Abstract: Glutathione (GSH) is an important factor in determining tolerance against oxidative stress in living organisms. It is synthesized in two sequential reactions catalyzed by [gamma]-glutamylcysteine synthetase (GCS) and glutathione synthetase (GS) in the presence of ATP. In this work, the effects of three different oxidative stresses were examined on GSH content and GSH-related enzyme activities in the fission yeast Schizosaccharomyces pombe. GSH content in S. pombe was significantly enhanced by treatment with hydrogen peroxide, [beta]-naphthoflavone (BNF) and tert-butylhydroquinone (BHQ). Simultaneously, they greatly induced GCS and GS activity. However, they did not have any effects on glutathione reductase activity. These results suggest that GCS and GS activities in S. pombe are upregulated by oxidative stress.

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