Bacteriostatic and Bactericidal Effects of Free Nitrous Acid on Model Microbes in Wastewater Treatment
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Photosynthetic Metabolism and Nitrogen Reshuffling Are Regulated
plants Article Photosynthetic Metabolism and Nitrogen Reshuffling Are Regulated by Reversible Cysteine Thiol Oxidation Following Nitrogen Deprivation in Chlamydomonas Amanda L. Smythers , Evan W. McConnell , Hailey C. Lewis, Saher N. Mubarek and Leslie M. Hicks * Department of Chemistry, The University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA; [email protected] (A.L.S.); [email protected] (E.W.M.); [email protected] (H.C.L.); [email protected] (S.N.M.) * Correspondence: [email protected]; Tel.: +1-919-843-6903 Received: 30 April 2020; Accepted: 19 June 2020; Published: 23 June 2020 Abstract: As global temperatures climb to historic highs, the far-reaching effects of climate change have impacted agricultural nutrient availability. This has extended to low latitude oceans, where a deficit in both nitrogen and phosphorus stores has led to dramatic decreases in carbon sequestration in oceanic phytoplankton. Although Chlamydomonas reinhardtii, a freshwater model green alga, has shown drastic systems-level alterations following nitrogen deprivation, the mechanisms through which these alterations are triggered and regulated are not fully understood. This study examined the role of reversible oxidative signaling in the nitrogen stress response of C. reinhardtii. Using oxidized cysteine resin-assisted capture enrichment coupled with label-free quantitative proteomics, 7889 unique oxidized cysteine thiol identifiers were quantified, with 231 significantly changing peptides from 184 proteins following 2 h of nitrogen deprivation. These results demonstrate that the cellular response to nitrogen assimilation, photosynthesis, pigment biosynthesis, and lipid metabolism are regulated by reversible oxidation. An enhanced role of non-damaging oxidative pathways is observed throughout the photosynthetic apparatus that provides a framework for further analysis in phototrophs. -
Quantification of Oxidative Stress Biomarkers: Development of a Method by Ultra Performance Liquid Chromatography MASTER DISSERTATION
DM Quantification of Oxidative Stress Biomarkers: Development of a Method by Ultra Performance Liquid Chromatography MASTER DISSERTATION Nome Autor do Liliana da Silva Rodrigues MASTER IN APPLIED BIOCHEMISTRY Quantification of Oxidative Stress Biomarkers: Development of a Method by Ultra Performance Liquid Chromatography Liliana da Silva Rodrigues July | 2016 Nome do Projecto/Relatório/Dissertação de Mestrado e/ou Tese de Doutoramento | Nome do Projecto/Relatório/Dissertação de Mestrado e/ou Tese DIMENSÕES: 45 X 29,7 cm NOTA* PAPEL: COUCHÊ MATE 350 GRAMAS Caso a lombada tenha um tamanho inferior a 2 cm de largura, o logótipo institucional da UMa terá de rodar 90º , para que não perca a sua legibilidade|identidade. IMPRESSÃO: 4 CORES (CMYK) ACABAMENTO: LAMINAÇÃO MATE Caso a lombada tenha menos de 1,5 cm até 0,7 cm de largura o laoyut da mesma passa a ser aquele que consta no lado direito da folha. Quantification of Oxidative Stress Biomarkers: Development of a Method by Ultra Performance Liquid Chromatography MASTER DISSERTATION Liliana da Silva Rodrigues MASTER IN APPLIED BIOCHEMISTRY ORIENTADORA Helena Caldeira Araújo CO-ORIENTADOR José de Sousa Câmara Quantification of oxidative stress biomarkers: Development of a Method by Ultra Performance Liquid Chromatography Dissertation submitted at the University of Madeira in order to obtain the degree of Master in Applied Biochemistry Liliana da Silva Rodrigues Work developed under the orientation of: Supervisor Prof. Doctor Helena Cardeira Araújo Co-supervisor Prof. Doctor José de Sousa Câmara Funchal, Portugal July 2016 To my Family “Sem eles nada disto seria possível” ***** Quantification of Oxidative Stress Biomarkers: Development of a Method by Ultra Performance Liquid Chromatography July 2016 Acknowledgment I would like to address an acknowledgement to all the people who collaborated in the accomplishment of this work. -
Sex Differences in the Genetic Architecture of Depression
www.nature.com/scientificreports OPEN Sex diferences in the genetic architecture of depression Hee-Ju Kang1,3, Yoomi Park2,3, Kyung-Hun Yoo2, Ki-Tae Kim2, Eun-Song Kim1, Ju-Wan Kim1, Sung-Wan Kim1, Il-Seon Shin1, Jin-Sang Yoon1, Ju Han Kim2,3 ✉ & Jae-Min Kim1,3 ✉ The prevalence and clinical characteristics of depressive disorders difer between women and men; however, the genetic contribution to sex diferences in depressive disorders has not been elucidated. To evaluate sex-specifc diferences in the genetic architecture of depression, whole exome sequencing of samples from 1000 patients (70.7% female) with depressive disorder was conducted. Control data from healthy individuals with no psychiatric disorder (n = 72, 26.4% female) and East-Asian subpopulation 1000 Genome Project data (n = 207, 50.7% female) were included. The genetic variation between men and women was directly compared using both qualitative and quantitative research designs. Qualitative analysis identifed fve genetic markers potentially associated with increased risk of depressive disorder in females, including three variants (rs201432982 within PDE4A, and rs62640397 and rs79442975 within FDX1L) mapping to chromosome 19p13.2 and two novel variants (rs820182 and rs820148) within MYO15B at the chromosome 17p25.1 locus. Depressed patients homozygous for these variants showed more severe depressive symptoms and higher suicidality than those who were not homozygotes (i.e., heterozygotes and homozygotes for the non-associated allele). Quantitative analysis demonstrated that the genetic burden of protein-truncating and deleterious variants was higher in males than females, even after permutation testing. Our study provides novel genetic evidence that the higher prevalence of depressive disorders in women may be attributable to inherited variants. -
A Novel Complex Neurological Phenotype Due to a Homozygous Mutation in FDX2
doi:10.1093/brain/awy172 BRAIN 2018: 141; 2289–2298 | 2289 Downloaded from https://academic.oup.com/brain/article-abstract/141/8/2289/5054138 by FAC.MED.RIB.PRETO-BIBL.CENTRAL-USP user on 26 October 2018 A novel complex neurological phenotype due to a homozygous mutation in FDX2 Juliana Gurgel-Giannetti,1,* David S. Lynch,2,3,* Anderson Rodrigues Branda˜o de Paiva,4 Leandro Tavares Lucato,5 Guilherme Yamamoto,6 Christer Thomsen,7 Somsuvro Basu,8 Fernando Freua,4 Alexandre Varella Giannetti,9 Bruno Della Ripa de Assis,4 Mara Dell Ospedale Ribeiro,4 Isabella Barcelos,4 Katiane Saya˜o Souza,4 Fernanda Monti,4 Uira´ Souto Melo,6 Simone Amorim,4 Leonardo G. L. Silva,6 Lu´cia Ineˆs Macedo-Souza,6 Angela M. Vianna-Morgante,6 Michio Hirano,10 Marjo S. Van der Knaap,11 Roland Lill,8,12 Mariz Vainzof,6 Anders Oldfors,7 Henry Houlden2,3 and Fernando Kok4,6 *These authors contributed equally to this work. Defects in iron–sulphur [Fe-S] cluster biogenesis are increasingly recognized as causing neurological disease. Mutations in a number of genes that encode proteins involved in mitochondrial [Fe-S] protein assembly lead to complex neurological phenotypes. One class of proteins essential in the early cluster assembly are ferredoxins. FDX2 is ubiquitously expressed and is essential in the de novo formation of [2Fe-2S] clusters in humans. We describe and genetically define a novel complex neurological syndrome identified in two Brazilian families, with a novel homozygous mutation in FDX2. Patients were clinically evaluated, underwent MRI, nerve conduction studies, EMG and muscle biopsy. -
Structure and Functional Dynamics of the Mitochondrial Fe/S Cluster Synthesis Complex
ARTICLE DOI: 10.1038/s41467-017-01497-1 OPEN Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex Michal T. Boniecki1, Sven A. Freibert 2, Ulrich Mühlenhoff2, Roland Lill 2,3 & Miroslaw Cygler 1,4 Iron–sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy conversion. De novo Fe/S cluster synthesis occurs on the mitochondrial scaffold protein ISCU and requires cysteine 1234567890 desulfurase NFS1, ferredoxin, frataxin, and the small factors ISD11 and ACP (acyl carrier protein). Both the mechanism of Fe/S cluster synthesis and function of ISD11-ACP are poorly understood. Here, we present crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU, and we use SAXS analyses to define the 3D architecture of the complete mitochondrial Fe/S cluster biosynthetic complex. Our structural and biochemical studies provide mechanistic insights into Fe/S cluster synthesis at the catalytic center defined by the active-site Cys of NFS1 and conserved Cys, Asp, and His residues of ISCU. We assign specific regulatory rather than catalytic roles to ISD11-ACP that link Fe/S cluster synthesis with mitochondrial lipid synthesis and cellular energy status. 1 Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK, Canada S7N 5E5. 2 Institut für Zytobiologie und Zytopathologie, Philipps-Universität, Robert-Koch-Strasse 6, 35032 Marburg, Germany. 3 LOEWE Zentrum für Synthetische Mikrobiologie SynMikro, Hans- Meerwein-Strasse, 35043 Marburg, Germany. 4 Department of Biochemistry, McGill University, 3649 Promenade Sir William Osler, Montreal, QC, Canada H3G 0B1. -
Antioxidant Properties of Catechins Comparison with Other Antioxidants
Food Chemistry 241 (2018) 480–492 Contents lists available at ScienceDirect Food Chemistry journal homepage: www.elsevier.com/locate/foodchem Antioxidant properties of catechins: Comparison with other antioxidants MARK ⁎ Michalina Grzesika, Katarzyna Naparłoa, Grzegorz Bartoszb, Izabela Sadowska-Bartosza, a Department of Analytical Biochemistry, Faculty of Biology and Agriculture, University of Rzeszów, ul. Zelwerowicza 4, 35-601 Rzeszów, Poland b Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Łódź, Pomorska 141/143, 90-236 Łódź, Poland ARTICLE INFO ABSTRACT Keywords: Antioxidant properties of five catechins and five other flavonoids were compared with several other natural and Catechins synthetic compounds and related to glutathione and ascorbate as key endogenous antioxidants in several in vitro % Flavonoids tests and assays involving erythrocytes. Catechins showed the highest ABTS -scavenging capacity, the highest FRAP stoichiometry of Fe3+ reduction in the FRAP assay and belonged to the most efficient compounds in protection Hemolysis against SIN-1 induced oxidation of dihydrorhodamine 123, AAPH-induced fluorescein bleaching and hypo- chlorite-induced fluorescein bleaching. Glutathione and ascorbate were less effective. (+)-catechin and (−)-epicatechin were the most effective compounds in protection against AAPH-induced erythrocyte hemolysis while (−)-epicatechin gallate, (−)-epigallocatechin gallate and (−)-epigallocatechin protected at lowest con- centrations against hypochlorite-induced -
Functional Reconstitution of Mitochondrial Fe/S Cluster Synthesis on Isu1 Reveals the Involvement of Ferredoxin
ARTICLE Received 18 May 2014 | Accepted 19 Aug 2014 | Published 31 Oct 2014 DOI: 10.1038/ncomms6013 Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin Holger Webert1, Sven-Andreas Freibert1, Angelo Gallo2, Torsten Heidenreich1, Uwe Linne3, Stefan Amlacher4, Ed Hurt4, Ulrich Mu¨hlenhoff1, Lucia Banci2,5 & Roland Lill1,6,7 Maturation of iron–sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe–2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and its reductase Arh1. The roles of Yah1–Arh1 have remained enigmatic, because they are not required for in vitro Fe/S cluster assembly. Here, we reconstitute [2Fe–2S] cluster synthesis on Isu1 in a reaction depending on Nfs1-Isd11, frataxin, Yah1, Arh1 and NADPH. Unlike in the bacterial system, frataxin is an essential part of Fe/S cluster biosynthesis and is required simultaneously and stoichiome- trically to Yah1. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1–apo-Isu1. Nuclear magnetic resonance structural studies identify the Yah1–apo-Isu1 interaction surface and suggest a pathway for electron flow from reduced ferredoxin to Isu1. Together, our study defines the molecular function of the ferre- doxin Yah1 and its human orthologue FDX2 in mitochondrial Fe/S cluster synthesis. 1 Institut fu¨r Zytobiologie und Zytopathologie, Philipps-Universita¨t Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany. 2 CERM, Magnetic Resonance Center, University of Florence, Sesto Fiorentino, 50019 Florence, Italy. 3 Fachbereich Chemie, Philipps-Universita¨t Marburg, Hans-Meerwein-Street, 35043 Marburg, Germany. -
On the Liquid Chemistry of the Reactive Nitrogen Species Peroxynitrite and Nitrogen Dioxide Generated by Physical Plasmas
biomolecules Article On the Liquid Chemistry of the Reactive Nitrogen Species Peroxynitrite and Nitrogen Dioxide Generated by Physical Plasmas Giuliana Bruno 1, Sebastian Wenske 1, Jan-Wilm Lackmann 2, Michael Lalk 3 , Thomas von Woedtke 4 and Kristian Wende 1,* 1 Centre for Innovation Competence (ZIK) Plasmatis, Leibniz Institute for Plasma Science and Technology (INP Greifswald), 17489 Greifswald, Germany; [email protected] (G.B.); [email protected] (S.W.) 2 Cluster of Excellence Cellular Stress Responses in Aging-Associated Diseases, University of Cologne, 50931 Cologne, Germany; [email protected] 3 Institute of Biochemistry, University of Greifswald, 17487 Greifswald, Germany; [email protected] 4 Leibniz Institute for Plasma Science and Technology, 17489 Greifswald, Germany; [email protected] * Correspondence: [email protected] Received: 9 November 2020; Accepted: 9 December 2020; Published: 16 December 2020 Abstract: Cold physical plasmas modulate cellular redox signaling processes, leading to the evolution of a number of clinical applications in recent years. They are a source of small reactive species, including reactive nitrogen species (RNS). Wound healing is a major application and, as its physiology involves RNS signaling, a correlation between clinical effectiveness and the activity of plasma-derived RNS seems evident. To investigate the type and reactivity of plasma-derived RNS in aqueous systems, a model with tyrosine as a tracer was utilized. By high-resolution mass spectrometry, 26 different tyrosine derivatives including the physiologic nitrotyrosine were identified. The product pattern was distinctive in terms of plasma parameters, especially gas phase composition. By scavenger experiments and isotopic labelling, gaseous nitric dioxide radicals and liquid phase peroxynitrite ions were determined as dominant RNS. -
WO 2013/066848 Al 10 May 2013 (10.05.2013) W P O PCT
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2013/066848 Al 10 May 2013 (10.05.2013) W P O PCT (51) International Patent Classification: SHETTY, Reshma P. [US/US]; 1506 Columbia Road, CUP 7/(94 (2006.01) Unit 4, Boston, Massachusetts 02127 (US). KELLY, Jason R. [US/US]; 29 Elm Street, Apt. 4, Cambridge, (21) International Application Number: Massachusetts 02139 (US). PCT/US20 12/062540 (74) Agent: CAMACHO, Jennifer A.; Greenberg Traurig, (22) International Filing Date: LLP, One International Place, Boston, Massachusetts 30 October 2012 (30.10.2012) 021 10 (US). (25) Filing Language: English (81) Designated States (unless otherwise indicated, for every (26) Publication Language: English kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (30) Priority Data: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, 13/285,919 3 1 October 201 1 (3 1. 10.201 1) US DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (71) Applicant: GINKGO BIOWORKS, INC. [US/US]; 27 HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, Drydock Avenue, Boston, Massachusetts 02210 (US). KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, (72) Inventors; and NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, (71) Applicants : FISCHER, Curt R [US/US]; 169 RW, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, Monsignor O'Brien Highway, #314, Cambridge, Mas TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, sachusetts 02141 (US). -
Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant
antioxidants Review Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species Dayana Benchoam 1,2, Ernesto Cuevasanta 1,2,3, Matías N. Möller 2,4 and Beatriz Alvarez 1,2,* 1 Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay; [email protected] (D.B.); [email protected] (E.C.) 2 Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo 11800, Uruguay; [email protected] 3 Unidad de Bioquímica Analítica, Centro de Investigaciones Nucleares, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay 4 Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay * Correspondence: [email protected] Received: 22 January 2019; Accepted: 19 February 2019; Published: 22 February 2019 – Abstract: Hydrogen sulfide (H2S/HS ) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH). Reactions with oxidized thiol products form persulfides (RSSH/RSS–). Persulfides have been proposed to transduce the signaling effects of H2S through the modification of critical cysteines. They are more nucleophilic and acidic than thiols and, contrary to thiols, also possess electrophilic character. In this review, we summarize the biochemistry of hydrogen sulfide and persulfides, focusing on redox aspects. We describe biologically relevant one- and two-electron oxidants and their reactions with H2S and persulfides, as well as the fates of the oxidation products. The biological implications are discussed. Keywords: hydrogen sulfide; persulfide; hydropersulfide; reactive oxygen species; sulfiyl radical 1. -
Chinese Medicine for Psoriasis Vulgaris Based on Syndrome Pattern: a Network Pharmacological Study
Hindawi Evidence-Based Complementary and Alternative Medicine Volume 2020, Article ID 5239854, 16 pages https://doi.org/10.1155/2020/5239854 Research Article Chinese Medicine for Psoriasis Vulgaris Based on Syndrome Pattern: A Network Pharmacological Study Dongmei Wang ,1,2,3 Chuanjian Lu ,2,3 Jingjie Yu,2,3 Miaomiao Zhang,2,3 Wei Zhu,2,3 and Jiangyong Gu 2,3,4 1Dermatology Hospital of Southern Medical University, Guangzhou 510091, China 2Guangdong Provincial Academy of Chinese Medical Sciences, Guangzhou 510006, China 3'e Second Clinical College, Guangzhou University of Chinese Medicine, Guangzhou 510006, China 4Department of Biochemistry, School of Basic Medical Science, Guangzhou University of Chinese Medicine, Guangzhou 510006, China Correspondence should be addressed to Chuanjian Lu; [email protected] and Jiangyong Gu; [email protected] Received 9 September 2019; Revised 13 January 2020; Accepted 23 January 2020; Published 28 April 2020 Academic Editor: Maria Camilla Bergonzi Copyright © 2020 Dongmei Wang et al. -is is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Background. -e long-term use of conventional therapy for psoriasis vulgaris remains a challenge due to limited or no patient response and severe side effects. Complementary and alternative treatments such as traditional Chinese medicine (TCM) are widely used in East Asia. TCM treatment is based on individual syndrome types. -ree TCM formulae, Compound Qingdai Pills (F1), Yujin Yinxie Tablets (F2), and Xiaoyin Tablets (F3), are used for blood heat, blood stasis, and blood dryness type of psoriasis vulgaris, respectively. -
GC-MS) Techniques and Selected Ion Flow Tube Mass Spectrometry (SIFT-MS) Assessment of Volatiles Produced from Nitric Oxide Producing Smart Dressings
The detection of trace volatiles from complex matrices using gas chromatography mass spectrometry (GC-MS) techniques and selected ion flow tube mass spectrometry (SIFT-MS) assessment of volatiles produced from nitric oxide producing smart dressings Oliver John Gould A thesis submitted in partial fulfilment of the requirements of the University of the West of England, Bristol for the degree of Doctor of Philosophy Faculty of Health and Applied Sciences, University of the West of England, Bristol 2019 Copyright declaration This copy has been supplied on the understanding that it is copyright material and that no quotation from the thesis may be published without proper acknowledgment. i Acknowledgements I would like to thank my supervisors Professor Norman Ratcliffe, and Associate Professor Ben de Lacy Costello for all their help, guidance, and support over the course of this work, and for their co-authorship on the published versions of chapters 2 and 3. I would also like to thank Dr Hugh Munro and Edixomed Ltd for financial support and scientific guidance with chapter 4. I would like to thank my co-authors on the publication of chapter 2 Tom Wieczorek, Professor Raj Persad. Also thank you to my co-authors on the publication of chapter 3, Amy Smart, Dr Angus Macmaster, and Dr Karen Ransley; and express my appreciation to Givaudan for funding the work undertaken in chapter 3. Thank you also to my colleagues and fellow post graduate research students at the University of the West of England for always being on hand for discussion and generation of ideas. A special mention to Dr Peter Jones who has been mentoring me on mass spectrometry for a number of years.