Ändra sökning
Avgränsa sökresultatet
1 - 29 av 29
RefereraExporteraLänk till träfflistan
Permanent länk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Träffar per sida
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sortering
  • Standard (Relevans)
  • Författare A-Ö
  • Författare Ö-A
  • Titel A-Ö
  • Titel Ö-A
  • Publikationstyp A-Ö
  • Publikationstyp Ö-A
  • Äldst först
  • Nyast först
  • Skapad (Äldst först)
  • Skapad (Nyast först)
  • Senast uppdaterad (Äldst först)
  • Senast uppdaterad (Nyast först)
  • Disputationsdatum (tidigaste först)
  • Disputationsdatum (senaste först)
  • Standard (Relevans)
  • Författare A-Ö
  • Författare Ö-A
  • Titel A-Ö
  • Titel Ö-A
  • Publikationstyp A-Ö
  • Publikationstyp Ö-A
  • Äldst först
  • Nyast först
  • Skapad (Äldst först)
  • Skapad (Nyast först)
  • Senast uppdaterad (Äldst först)
  • Senast uppdaterad (Nyast först)
  • Disputationsdatum (tidigaste först)
  • Disputationsdatum (senaste först)
Markera
Maxantalet träffar du kan exportera från sökgränssnittet är 250. Vid större uttag använd dig av utsökningar.
  • 1.
    Enmark, Martin
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013). Uppsala University.
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Samuelsson, Jörgen
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Örnskov, Eivor
    IMED Biotech Unit, Sweden.
    Schweikart, Fritz
    IMED Biotech Unit, Sweden.
    Fornstedt, Torgny
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Investigation of factors influencing the separation of diastereomers of phosphorothioated oligonucleotides2019Ingår i: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 411, nr 15, s. 3383-3394Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    This study presents a systematic investigation of factors influencing the chromatographic separation of diastereomers of phosphorothioated pentameric oligonucleotides as model solutes. Separation was carried out under ion-pairing conditions using an XBridge C18 column. For oligonucleotides with a single sulfur substitution, the diastereomer selectivity was found to increase with decreasing carbon chain length of the tertiary alkylamine used as an ion-pair reagent. Using an ion-pair reagent with high selectivity for diastereomers, triethylammonium, it was found the selectivity increased with decreased ion-pair concentration and shallower gradient slope. Selectivity was also demonstrated to be dependent on the position of the modified linkage. Substitutions at the center of the pentamer resulted in higher diastereomer selectivity compared to substitutions at either end. For mono-substituted oligonucleotides, the retention order and stereo configuration were consistently found to be correlated, with Rp followed by Sp, regardless of which linkage was modified. The type of nucleobase greatly affects the observed selectivity. A pentamer of cytosine has about twice the diastereomer selectivity of that of thymine. When investigating the retention of various oligonucleotides eluted using tributylammonium as the ion-pairing reagent, no diastereomer selectivity could be observed. However, retention was found to be dependent on both the degree and position of sulfur substitution as well as on the nucleobase. When analyzing fractions collected in the front and tail of overloaded injections, a significant difference was found in the ratio between Rp and Sp diastereomers, indicating that the peak broadening observed when using tributylammonium could be explained by partial diastereomer separation.

  • 2.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Goetelen, T
    Fors, E
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Anoxic induction of the chlorite dismutase gene of Ideonella dechloratans is dependent of the fumarate and nitrate reduction regulatorManuskript (preprint) (Övrigt vetenskapligt)
  • 3.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Johansson, Nicklas
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Expression of Chlorite Dismutase and Chlorate Reductase in the Prescence of Oxygen and/or Chlorate as the Terminal Electron Acceptor in Ideonella dechloratans2012Ingår i: Applied and Environmental Microbiology, ISSN 0099-2240, E-ISSN 1098-5336, Vol. 78, nr 12, s. 4380-4385Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The ability of microorganisms to perform dissimilatory (per)chlorate reduction is, for most species, known to be oxygen sensitive. Consequently, bioremediation processes for the removal of oxochlorates will be disturbed if oxygen is present. We measured the expression of chlorite dismutase and chlorate reductase in the presence of different terminal electron acceptors in the chlorate reducer Ideonella dechloratans. Enzyme activity assays and mRNA analyses by real-time quantitative reverse transcription (qRT)-PCR were performed on cell extracts from cells grown aerobically with and without chlorate and on cells grown anaerobically in the presence of chlorate. Our results showed that both chlorite dismutase and chlorate reductase are expressed during aerobic growth. However, transfer to anaerobic conditions with chlorate resulted in significantly enhanced enzyme activities and mRNA levels for both enzymes. Absence of oxygen was necessary for the induction to occur, since chlorate addition under aerobic conditions produced neither increased enzyme activities nor higher relative levels of mRNA. For chlorite dismutase, the observed increase in activity was on the same order of magnitude as the increase in the relative mRNA level, indicating gene regulation at the transcriptional level. However, chlorate reductase showed about 200 times higher enzyme activity in anaerobically induced cells, whereas the increase in mRNA was only about 10-fold, suggesting additional mechanisms influence the enzyme activity.

  • 4.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    An Fnr-type transcriptional regulator is responsible for anoxic up-regulation of chlorite dismutase in Ideonella dechloratansManuskript (preprint) (Övrigt vetenskapligt)
  • 5.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Expression of chlorate reductase and chlorite dismutase in the chlorate-respiring bacterium Ideonella dechloratans2012Konferensbidrag (Övrigt vetenskapligt)
  • 6.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Expression of the gene cluster for chlorate metabolism in the chlorate-respiring bacterium Ideonella dechloratans2012Ingår i: Biochimica et Biophysica Acta Bioenergetics, Volume 1817, Supplement, October 2012: EBEC Abstract Book / [ed] Friedrich T., Einsle O., Gräber P., Frankfurt, 2012, s. S157-S158Konferensbidrag (Övrigt vetenskapligt)
    Abstract [en]

    Ideonella dechloratans is a facultative anaerobe able to use chlorate as a terminal electron acceptor under anaerobic conditions. Two enzymes are necessary for the decomposition of chlorate to chloride and molecular oxygen; chlorate reductase (Clr) and chlorite dismutase (Cld).  The genes for these two enzymes are close to each other in the genome and form, together with a cytochrome c and a mob B gene, a gene cluster for chlorate metabolism. The localization of the cyt c gene suggests a function in electron transport during chlorate reduction but the corresponding protein has not been found. We have addressed the questions of how the expression of Cld and Clr is regulated during the aerob/anaerob switch and if the cyt c gene is expressed in I. dechloratans. The enzyme activities of Cld and Clr were measured in extracts from cells grown at different conditions; aerobically or anaerobically [1]. Both enzymes were found to be active in all samples and the activity increased upon transfer of the cells from aerobic to anaerobic conditions, by five times for Cld and more than 200 times for Clr. Relative mRNA levels of Cld and Clr were determined by qRT-PCR in RNA preparations from cells grown under the same conditions as for the enzyme activity measurements. mRNA from both genes was detected in all preparations but with ten times higher levels in samples from anaerobic conditions. This increase in mRNA level is on the same scale as the increase in enzyme activity for Cld but accounts for less than a tenth of the activity enhancement seen for Clr.  A possible effect of chlorate was tested by the addition of chlorate under aerobic conditions but this resulted in neither increased enzyme activities nor increased mRNA levels. qRT-PCR was performed with primers specific for the cyt c gene and this gene was also found to be expressed at both aerobic and anaerobic conditions. In summary, the results show that chlorate respiration is activated by anaero­biosis but not by chlorate in I. dechloratans and that this activation occurs at the tran­scriptional level. Due to the much larger increase in enzyme activity compared to the increase in mRNA level, the activity of Clr also seems to be effected by other mechanisms. Detection of cyt c mRNA suggests that its gene product can be found and the function investigated.

    [1] Hellberg Lindqvist M, Johansson N, Nilsson T, Rova M (2012) Appl. Environ. Microbiol. 78: 4380-4385

  • 7.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper (from 2013).
    Expression of the gene cluster for chlorate metabolism in the chlorate-respiring bacterium Ideonella dechloratans2012Ingår i: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1817, s. 157-158Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Ideonella dechloratans is a facultative anaerobe able to use chlorate as a terminal electron acceptor under anaerobic conditions. Two enzymes are necessary for the decomposition of chlorate to chloride and molecular oxygen; chlorate reductase (Clr) and chlorite dismutase (Cld). The genes for these two enzymes are close to each other in the genome and form, together with a cytochrome c and a mob B gene, a gene cluster for chlorate metabolism. The localization of the cyt c gene suggests a function in electron transport during chlorate reduction but the corresponding protein has not been found. We have addressed the questions of how the expression of Cld and Clr is regulated during the aerob/anaerob switch and if the cyt c gene is expressed in I. dechloratans. The enzyme activities of Cld and Clr were measured in extracts from cells grown at different conditions; aerobically or anaerobically [1]. Both enzymes were found to be active in all samples and the activity increased upon transfer of the cells from aerobic to anaerobic conditions, by five times for Cld and more than 200 times for Clr. Relative mRNA levels of Cld and Clr were determined by qRT-PCR in RNA preparations from cells grown under the same conditions as for the enzyme activity measurements. mRNA from both genes was detected in all preparations but with ten times higher levels in samples from anaerobic conditions. This increase in mRNA level is on the same scale as the increase in enzyme activity for Cld but accounts for less than a tenth of the activity enhancement seen for Clr. A possible effect of chlorate was tested by the addition of chlorate under aerobic conditions but this resulted in neither increased enzyme activities nor increased mRNA levels. qRT-PCR was performed with primers specific for the cyt c gene and this gene was also found to be expressed at both aerobic and anaerobic conditions. In summary, the results show that chlorate respiration is activated by anaerobiosis but not by chlorate in I. dechloratans and that this activation occurs at the transcriptional level. Due to the much larger increase in enzyme activity compared to the increase in mRNA level, the activity of Clr also seems to be effected by other mechanisms. Detection of cyt c mRNA suggests that its gene product can be found and the function investigated.

  • 8.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Regulation of genes involved in microbial degradation of chlorate in the chlorate-respiring bacterium Ideonella dechloratans.2013Konferensbidrag (Övrigt vetenskapligt)
    Abstract [en]

    Regulation of genes involved in microbial degradation of chlorate in the chlorate-respiring bacterium Ideonella dechloratans

    Ideonella dechloratans is a facultative anaerobe and can use both oxygen and chlorate as terminal electron acceptors. Chlorate metabolism involves two enzymes; chlorate reductase (Clr) and chlorite dismutase (Cld). The genes are located in a cluster for chlorate metabolism that also includes the genes for a cytochrome c and a mob B gene. A possible function of the cyt c gene is electron transport during chlorate reduction but so far no corresponding protein has been found. Our aim is to study the expression and possible regulation of Cld and Clr during aerobic and anaerobic metabolism and to examine if the cytochrome c is expressed in I. dechloratans. We have previously reported expression of Clr and Cld, measured both at the mRNA level and as enzyme activities (1). In order to examine sequences important for gene regulation the upstream regions of Clr and Cld were cloned and inserted in a reporter vector and transformed into E. coli XL-1 Blue. The expression of the cyt c gene was analyzed with qRT-PCR in RNA preparations from cells grown under different growth conditions; aerobically or anaerobically. Our results show that the cloned upstream regions of Clr and Cld include functional promoter sequences and that cyt c is expressed in I. dechloratans with increased levels at growth without an external oxygen supply.

    1.            Lindqvist, M. H., N. Johansson, T. Nilsson, and M. Rova. 2012. Expression of Chlorite Dismutase and Chlorate Reductase in the Presence of Oxygen and/or Chlorate as the Terminal Electron Acceptor in Ideonella dechloratans. Appl. Environ. Microbiol. 78:4380-4385.

     

  • 9.
    Hellberg Lindqvist, Miriam
    et al.
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Sundin, P
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Rova, Maria
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för ingenjörs- och kemivetenskaper.
    Chlorate reductase is cotranscribed with cytochrome c and other downstream genes in the gene cluster for chlorate respiration of Ideonella dechloratans2015Ingår i: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 362, nr 6Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The chlorate-respiring bacterium Ideonella dechloratans is a facultative anaerobe that can use both oxygen and chlorate as terminal electron acceptors. The genes for the enzymes chlorate reductase (clrABDC) and chlorite dismutase, necessary for chlorate metabolism and probably acquired by lateral gene transfer, are located in a gene cluster that also includes other genes potentially important for chlorate metabolism. Among those are a gene for cytochrome c (cyc) whose gene product may serve as an electron carrier during chlorate reduction, a cofactor biosynthesis gene (mobB) and a predicted transcriptional regulator (arsR). Only chlorate reductase and chlorite dismutase have been shown to be expressed in vivo. Here, we report the in vivo production of a single polycistronic transcript covering eight open reading frames including clrABDC, cyc, mobB and arsR. Transcription levels of the cyc and clrA genes were compared to each other by the use of qRT-PCR in RNA preparations from cells grown under aerobic or chlorate reducing anaerobic conditions. The two genes showed the same mRNA levels under both growth regimes, indicating that no transcription termination occurs between them. Higher transcription levels were observed at growth without external oxygen supply. Implications for electron pathway integration following lateral gene transfer are discussed.

  • 10.
    Hellberg, Miriam
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Nilsson, Thomas
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Johansson, Nicklas
    Regulation of the genes for chlorate reductase (Clr) and chlorite dismutase (Cld) in the chlorate-respiring bacterium Ideonella dechloratans2010Ingår i: FEBS Journal 277(2010) Supplement 1. Poster presentations, Wiley-Blackwell , 2010, s. B4.62.-Konferensbidrag (Övrigt vetenskapligt)
    Abstract [en]

    Enzyme activities and mRNA levels of chlorate reductase and chlorite dismutase was investigated in whole cell extracts of Ideonella dechloratans grown under different growth conditions. This bacterium grows well both at aerobic and anaerobic conditions, using oxygen and chlorate, respectively, as a terminal electron acceptor. It was found that preparations from cells grown in the absence of chlorate under aerobic conditions showed activity of both chlorate reductase, measured as chlorate dependent reduction of methyl viologen, and chlorite dismutase, measured as chlorite dependent oxygen production. At aerobic growth conditions, the addition of chlorate resulted in an increased activity of chlorate reductase. The highest activity of chlorate reductase was found in preparations from cells grown anaerobically in the presence of chlorate. No increase in enzyme activity could be detected for chlorite dismutase during anaerobic or aerobic growth in the presence of chlorate, compared to aerobic growth in the absence of chlorate. The mRNA levels for Clr and Cld, measured by real-time quantitative PCR using 16SrRNA as an intern standard, was found to be equal in preparations from cells grown anaerobically in the presence of chlorate compared to cells grown under aerobic conditions in the absence of chlorate. The results suggest that, in I. dechloratans, the activity of chlorate reductase is up-regulated by at least two factors, anaerobiosis and the presence of chlorate. Interestingly, the results also indicate that the studied regulation occurs at post-transcriptional level, while most examples of oxygen regulation in bacteria are reported to occur at transcriptional level.  

  • 11.
    Nilsson, Thomas
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Smedja Bäcklund, Anna
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Microbial metabolism of oxochlorates: A bioenergetic perspective2013Ingår i: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1827, nr 2, s. 189-197Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    The microbial metabolism of oxochlorates is part of the biogeochemical cycle of chlorine. Organisms capable of growth using perchlorate or chlorate as respiratory electron acceptors are also interesting for applications in biotreatment of oxochlorate-containing effluents or bioremediation of contaminated areas. In this review, we discuss the reactions of oxochlorate respiration, the corresponding enzymes, and the relation to respiratory electron transport that can contribute to a proton gradient across the cell membrane. Enzymes specific for oxochlorate respiration are oxochlorate reductases and chlorite dismutase. The former belong to DMSO reductase family of molybdenum-containing enzymes. The heme protein chlorite dismutase, which decomposes chlorite into chloride and molecular oxygen, is only distantly related to other proteins with known functions. Pathways for electron transport may be different in perchlorate and chlorate reducers, but appear in both cases to be similar to pathways found in other respiratory systems.

  • 12.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Balance between photoactivation and photoinhibition of photosystem II in Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit1995Konferensbidrag (Refereegranskat)
  • 13.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Changes in the oxidation state of cytochrome b-559 and tyrosine-D during in vivo photoactivation of phgotosystem II1998Ingår i: Garab, G (ed.) Photosynthesis:Mechanisms and Effects, Vol II pp 1097-1100,Artikel i tidskrift (Refereegranskat)
  • 14.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Coupled modification of the acceptor side of photosystem II during photoactivation of the oxygen evolving complex1998Rapport (Övrigt vetenskapligt)
  • 15.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Coupled modification of the acceptor-side of photosystem II during photoactivation of the oxygen evolving complex1998Rapport (Övrigt vetenskapligt)
  • 16.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Photoactivation and photoinhibition of photosystem II in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit1995Övrigt (Övrig (populärvetenskap, debatt, mm))
  • 17.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Photoactivation is less efficient in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit of Photosystem II1996Övrigt (Övrig (populärvetenskap, debatt, mm))
  • 18.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Protection of photosystem II from Photodamage during the Assembly of the Water Oxidizing Complex1999Ingår i: Ph.D. Thesis, Lund UniversityArtikel i tidskrift (Refereegranskat)
  • 19.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Studies of oxygen evolution and photoinhibition in a photosystem II mutant of Chlamydomonas reinhardtii1993Rapport (Övrigt vetenskapligt)
  • 20.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Studies of oxygen evolution and photoinhibition in a photosystem II mutant of Chlamydomonas reinhardtii1993Rapport (Övrigt vetenskapligt)
  • 21.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    The 23 kDa extrinsic subunit of PS II is essential for efficient photoactivation1996Övrigt (Övrig (populärvetenskap, debatt, mm))
  • 22.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    The balance between photoactivation and photoinhibition studied in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit of PS II1994Rapport (Övrigt vetenskapligt)
  • 23.
    Rova, Maria
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    The interrelationship between photoactivation and photoinhibition in a mutand of Chlamydomonas reinhardtii lacking the 23 kDa psb P protein of photosystem II1994Rapport (Övrigt vetenskapligt)
  • 24.
    Rova, Maria
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Franzén, Lars-Gunnar
    Department of Biochemistry, Arrhenius laboratories of Natural Science.
    Fredriksson, Per-Olof
    Styring, Stenbjörn
    Photosystem II in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa psb protein shows increased sensitivity to photoinhibition in the absence of chloride1994Ingår i: Photosynthesis Research, Vol. 39, nr 1, s. 77-83-Artikel i tidskrift (Refereegranskat)
  • 25.
    Rova, Maria
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Franzén, Lars-Gunnar
    Fredriksson, Per-Olof
    Styring, Stenbjörn
    Photosystem II in a mutant of Chlamydomonas reinhardtii lacking the 23kDa psbP protein shows increased sensitivity to photoinhibition in the absence of chloride1994Ingår i: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 39, s. 75-83Artikel i tidskrift (Refereegranskat)
  • 26.
    Rova, Maria
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Mamedov, Fikret
    Magnusson, Ann
    Fredriksson, Per-Olof
    Styring, Stenbjörn
    Coupled Activation of the Donor and the Acceptor Side of Photosystem II during Photoactivation of the Oxygen Evolving Cluster1998Ingår i: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 37, s. 11039-11045Artikel i tidskrift (Refereegranskat)
  • 27.
    Rova, Maria
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Mc Ewen, Birgitta
    Karlstads universitet, Fakulteten för hälsa, natur- och teknikvetenskap (from 2013), Institutionen för miljö- och livsvetenskaper.
    Fredriksson, Per-Olof
    Styring, Stenbjörn
    Balance between photoactivation and photoinhibition of photosystem II in Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit1995Konferensbidrag (Övrig (populärvetenskap, debatt, mm))
  • 28.
    Rova, Maria
    et al.
    Karlstads universitet, Fakulteten för teknik- och naturvetenskap, Avdelningen för kemi och biomedicinsk vetenskap.
    Mc Ewen, Birgitta
    Karlstads universitet, Institutionen för natur och miljö.
    Fredriksson, Per-Olof
    Styring, Stenbjörn
    Photoactivation and Photoinhibition Are Competing in a Mutant of Chlamydomonas reinhardtii Lacking the 23-kDa Extrinsic Subunit of Photosystem II1996Ingår i: The Journal of Biological Chemistry, Vol. 271, nr 46, s. 28918-28924Artikel i tidskrift (Refereegranskat)
  • 29.
    Rova, Maria
    et al.
    Karlstads universitet, Institutionen för kemi.
    Mc Ewen, Birgitta
    Karlstads universitet, Institutionen för natur och miljö.
    Fredriksson, Per-Olof
    Karlstads universitet, Institutionen för kemi.
    Styring, Stenbjörn
    Section of Chemistry, Uppsala University, Uppsala.
    Photoactivation and photoinhibition of photosystem II in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit1996Ingår i: Photosynthesis - From Light to Biosphere: Proceedings of the 10th International congress, Montpellier, France, 20-25 August 1995. Vol 2 / [ed] Mathis, Paul, Dortrecht: Kluwer Academic Publishers, 1996, s. 291-294Konferensbidrag (Övrigt vetenskapligt)
1 - 29 av 29
RefereraExporteraLänk till träfflistan
Permanent länk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf