Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria)
This study investigated the role of a novel metal-dependent catalase (Npun_R4582) that reduces hydrogen peroxide in the cyanobacterium Nostoc punctiforme . Quantitative real-time PCR showed that npun_R4582 relative mRNA levels were upregulated by over 16-fold in cells treated with either 2 μM added...
Gespeichert in:
| Veröffentlicht in: | Applied microbiology and biotechnology 2017-05, Vol.101 (9), p.3781-3800 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3800 |
|---|---|
| container_issue | 9 |
| container_start_page | 3781 |
| container_title | Applied microbiology and biotechnology |
| container_volume | 101 |
| creator | Hudek, L. Torriero, A. A. J. Michalczyk, A. A. Neilan, B. A. Ackland, M. L. Bräu, Lambert |
| description | This study investigated the role of a novel metal-dependent catalase (Npun_R4582) that reduces hydrogen peroxide in the cyanobacterium
Nostoc punctiforme
. Quantitative real-time PCR showed that
npun_R4582
relative mRNA levels were upregulated by over 16-fold in cells treated with either 2 μM added Co, 0.5 μM added Cu, 500 μM Mn, 1 μM Ni, or 18 μM Zn. For cells treated with 60 μM H
2
O
2
, no significant alteration in
Npun_R4582
relative mRNA levels was detected, while in cells treated with Co, Cu, Mn, Ni, or Zn and 60 μM peroxide, relative mRNA levels were generally above control or peroxide only treated cells. Disruption or overexpression of
npun_R4582
altered sensitivity to cells exposed to 60 μM H
2
O
2
and metals for treatments beyond the highest viable concentrations, or in a mixed metal solution for Npun_R4582
−
cells. Moreover, overexpression of
npun_R4582
increased cellular peroxidase activity in comparison with wild-type and Npun_R4582
−
cells, and reduced peroxide levels by over 50%. The addition of cobalt, manganese, nickel, and zinc increased the capacity of Npun_R4582 to reduce the rate or total levels of peroxide produced by cells growing under photooxidative conditions. The work presented confirms the function of NpunR4582 as a catalase and provides insights as to how cells reduce potentially lethal peroxide levels produced by photosynthesis. The findings also show how trace elements play crucial roles as enzymatic cofactors and how the role of Npun_R4582 in hydrogen peroxide breakdown is dependent on the type of metal and the level available to cells. |
| doi_str_mv | 10.1007/s00253-017-8130-y |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_journals_1889306147</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A550919033</galeid><sourcerecordid>A550919033</sourcerecordid><originalsourceid>FETCH-LOGICAL-c510t-c1ee267eae7e36745eeadd7be1093476d49553949e917a08917c47567df7b9ed3</originalsourceid><addsrcrecordid>eNp1kV1rHCEUhqU0NJu0P6A3RehNc2Gq4ziOlyG0TSA0pV-34uiZxbCjW3Ug8-_rsknahRZBUZ_nyPFF6DWj54xS-T5T2ghOKJOkZ5yS5RlasZY3hHasfY5W9UIQKVR_jE5yvqOUNX3XvUDHTc9EdbsV-vkFUrz3DnACN9viY8DDgg2eoJgNcbCF4CAUbE3dmwzYB_w55hIt3s6hCmNME-B3djEhDsYWSN6cvURHo9lkePWwnqIfHz98v7wiN7efri8vbogVjBZiGUDTSTAggXeyFQDGOTkAo4q3snOtEoKrVoFi0tC-zraVopNulIMCx0_R233dbYq_ZshF38U5hfqkZn2v-O4j5B9qbTagfRhjScZOPlt9IQRVTFHOK3X-D6oOB5O3McDo6_mBcHYgVKbAfVmbOWd9_e3rIcv2rE0x5wSj3iY_mbRoRvUuTL0PU9fM9C5MvVTnzUNz8zCBezIe06tAswdyvQprSH91_9-qvwFSZKen</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1889306147</pqid></control><display><type>article</type><title>Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria)</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Hudek, L. ; Torriero, A. A. J. ; Michalczyk, A. A. ; Neilan, B. A. ; Ackland, M. L. ; Bräu, Lambert</creator><creatorcontrib>Hudek, L. ; Torriero, A. A. J. ; Michalczyk, A. A. ; Neilan, B. A. ; Ackland, M. L. ; Bräu, Lambert</creatorcontrib><description>This study investigated the role of a novel metal-dependent catalase (Npun_R4582) that reduces hydrogen peroxide in the cyanobacterium
Nostoc punctiforme
. Quantitative real-time PCR showed that
npun_R4582
relative mRNA levels were upregulated by over 16-fold in cells treated with either 2 μM added Co, 0.5 μM added Cu, 500 μM Mn, 1 μM Ni, or 18 μM Zn. For cells treated with 60 μM H
2
O
2
, no significant alteration in
Npun_R4582
relative mRNA levels was detected, while in cells treated with Co, Cu, Mn, Ni, or Zn and 60 μM peroxide, relative mRNA levels were generally above control or peroxide only treated cells. Disruption or overexpression of
npun_R4582
altered sensitivity to cells exposed to 60 μM H
2
O
2
and metals for treatments beyond the highest viable concentrations, or in a mixed metal solution for Npun_R4582
−
cells. Moreover, overexpression of
npun_R4582
increased cellular peroxidase activity in comparison with wild-type and Npun_R4582
−
cells, and reduced peroxide levels by over 50%. The addition of cobalt, manganese, nickel, and zinc increased the capacity of Npun_R4582 to reduce the rate or total levels of peroxide produced by cells growing under photooxidative conditions. The work presented confirms the function of NpunR4582 as a catalase and provides insights as to how cells reduce potentially lethal peroxide levels produced by photosynthesis. The findings also show how trace elements play crucial roles as enzymatic cofactors and how the role of Npun_R4582 in hydrogen peroxide breakdown is dependent on the type of metal and the level available to cells.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-017-8130-y</identifier><identifier>PMID: 28150026</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Applied Microbial and Cell Physiology ; Astrobiology ; Bacteria ; Biomedical and Life Sciences ; Biotechnology ; Catalase - genetics ; Catalase - metabolism ; Catalysis ; Cobalt ; Coenzymes - metabolism ; Cyanobacteria ; Environmental science ; Enzymes ; Gene Deletion ; Gene Expression ; Gene Expression Profiling ; Hydrogen peroxide ; Investigations ; Life Sciences ; Manganese ; Metal concentrations ; Metals ; Metals - metabolism ; Microbial Genetics and Genomics ; Microbiology ; Nickel ; Nostoc - enzymology ; Nostoc - metabolism ; Oxidative stress ; Peroxides - metabolism ; Peroxides - toxicity ; Photosynthesis ; Real-Time Polymerase Chain Reaction ; RNA ; Studies ; Trace elements ; Zinc</subject><ispartof>Applied microbiology and biotechnology, 2017-05, Vol.101 (9), p.3781-3800</ispartof><rights>Springer-Verlag Berlin Heidelberg 2017</rights><rights>COPYRIGHT 2017 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-c1ee267eae7e36745eeadd7be1093476d49553949e917a08917c47567df7b9ed3</citedby><cites>FETCH-LOGICAL-c510t-c1ee267eae7e36745eeadd7be1093476d49553949e917a08917c47567df7b9ed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-017-8130-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-017-8130-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28150026$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hudek, L.</creatorcontrib><creatorcontrib>Torriero, A. A. J.</creatorcontrib><creatorcontrib>Michalczyk, A. A.</creatorcontrib><creatorcontrib>Neilan, B. A.</creatorcontrib><creatorcontrib>Ackland, M. L.</creatorcontrib><creatorcontrib>Bräu, Lambert</creatorcontrib><title>Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria)</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>This study investigated the role of a novel metal-dependent catalase (Npun_R4582) that reduces hydrogen peroxide in the cyanobacterium
Nostoc punctiforme
. Quantitative real-time PCR showed that
npun_R4582
relative mRNA levels were upregulated by over 16-fold in cells treated with either 2 μM added Co, 0.5 μM added Cu, 500 μM Mn, 1 μM Ni, or 18 μM Zn. For cells treated with 60 μM H
2
O
2
, no significant alteration in
Npun_R4582
relative mRNA levels was detected, while in cells treated with Co, Cu, Mn, Ni, or Zn and 60 μM peroxide, relative mRNA levels were generally above control or peroxide only treated cells. Disruption or overexpression of
npun_R4582
altered sensitivity to cells exposed to 60 μM H
2
O
2
and metals for treatments beyond the highest viable concentrations, or in a mixed metal solution for Npun_R4582
−
cells. Moreover, overexpression of
npun_R4582
increased cellular peroxidase activity in comparison with wild-type and Npun_R4582
−
cells, and reduced peroxide levels by over 50%. The addition of cobalt, manganese, nickel, and zinc increased the capacity of Npun_R4582 to reduce the rate or total levels of peroxide produced by cells growing under photooxidative conditions. The work presented confirms the function of NpunR4582 as a catalase and provides insights as to how cells reduce potentially lethal peroxide levels produced by photosynthesis. The findings also show how trace elements play crucial roles as enzymatic cofactors and how the role of Npun_R4582 in hydrogen peroxide breakdown is dependent on the type of metal and the level available to cells.</description><subject>Applied Microbial and Cell Physiology</subject><subject>Astrobiology</subject><subject>Bacteria</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Catalase - genetics</subject><subject>Catalase - metabolism</subject><subject>Catalysis</subject><subject>Cobalt</subject><subject>Coenzymes - metabolism</subject><subject>Cyanobacteria</subject><subject>Environmental science</subject><subject>Enzymes</subject><subject>Gene Deletion</subject><subject>Gene Expression</subject><subject>Gene Expression Profiling</subject><subject>Hydrogen peroxide</subject><subject>Investigations</subject><subject>Life Sciences</subject><subject>Manganese</subject><subject>Metal concentrations</subject><subject>Metals</subject><subject>Metals - metabolism</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Nickel</subject><subject>Nostoc - enzymology</subject><subject>Nostoc - metabolism</subject><subject>Oxidative stress</subject><subject>Peroxides - metabolism</subject><subject>Peroxides - toxicity</subject><subject>Photosynthesis</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>RNA</subject><subject>Studies</subject><subject>Trace elements</subject><subject>Zinc</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kV1rHCEUhqU0NJu0P6A3RehNc2Gq4ziOlyG0TSA0pV-34uiZxbCjW3Ug8-_rsknahRZBUZ_nyPFF6DWj54xS-T5T2ghOKJOkZ5yS5RlasZY3hHasfY5W9UIQKVR_jE5yvqOUNX3XvUDHTc9EdbsV-vkFUrz3DnACN9viY8DDgg2eoJgNcbCF4CAUbE3dmwzYB_w55hIt3s6hCmNME-B3djEhDsYWSN6cvURHo9lkePWwnqIfHz98v7wiN7efri8vbogVjBZiGUDTSTAggXeyFQDGOTkAo4q3snOtEoKrVoFi0tC-zraVopNulIMCx0_R233dbYq_ZshF38U5hfqkZn2v-O4j5B9qbTagfRhjScZOPlt9IQRVTFHOK3X-D6oOB5O3McDo6_mBcHYgVKbAfVmbOWd9_e3rIcv2rE0x5wSj3iY_mbRoRvUuTL0PU9fM9C5MvVTnzUNz8zCBezIe06tAswdyvQprSH91_9-qvwFSZKen</recordid><startdate>20170501</startdate><enddate>20170501</enddate><creator>Hudek, L.</creator><creator>Torriero, A. A. J.</creator><creator>Michalczyk, A. A.</creator><creator>Neilan, B. A.</creator><creator>Ackland, M. L.</creator><creator>Bräu, Lambert</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20170501</creationdate><title>Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria)</title><author>Hudek, L. ; Torriero, A. A. J. ; Michalczyk, A. A. ; Neilan, B. A. ; Ackland, M. L. ; Bräu, Lambert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-c1ee267eae7e36745eeadd7be1093476d49553949e917a08917c47567df7b9ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Applied Microbial and Cell Physiology</topic><topic>Astrobiology</topic><topic>Bacteria</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Catalase - genetics</topic><topic>Catalase - metabolism</topic><topic>Catalysis</topic><topic>Cobalt</topic><topic>Coenzymes - metabolism</topic><topic>Cyanobacteria</topic><topic>Environmental science</topic><topic>Enzymes</topic><topic>Gene Deletion</topic><topic>Gene Expression</topic><topic>Gene Expression Profiling</topic><topic>Hydrogen peroxide</topic><topic>Investigations</topic><topic>Life Sciences</topic><topic>Manganese</topic><topic>Metal concentrations</topic><topic>Metals</topic><topic>Metals - metabolism</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Nickel</topic><topic>Nostoc - enzymology</topic><topic>Nostoc - metabolism</topic><topic>Oxidative stress</topic><topic>Peroxides - metabolism</topic><topic>Peroxides - toxicity</topic><topic>Photosynthesis</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>RNA</topic><topic>Studies</topic><topic>Trace elements</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hudek, L.</creatorcontrib><creatorcontrib>Torriero, A. A. J.</creatorcontrib><creatorcontrib>Michalczyk, A. A.</creatorcontrib><creatorcontrib>Neilan, B. A.</creatorcontrib><creatorcontrib>Ackland, M. L.</creatorcontrib><creatorcontrib>Bräu, Lambert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hudek, L.</au><au>Torriero, A. A. J.</au><au>Michalczyk, A. A.</au><au>Neilan, B. A.</au><au>Ackland, M. L.</au><au>Bräu, Lambert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria)</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2017-05-01</date><risdate>2017</risdate><volume>101</volume><issue>9</issue><spage>3781</spage><epage>3800</epage><pages>3781-3800</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>This study investigated the role of a novel metal-dependent catalase (Npun_R4582) that reduces hydrogen peroxide in the cyanobacterium
Nostoc punctiforme
. Quantitative real-time PCR showed that
npun_R4582
relative mRNA levels were upregulated by over 16-fold in cells treated with either 2 μM added Co, 0.5 μM added Cu, 500 μM Mn, 1 μM Ni, or 18 μM Zn. For cells treated with 60 μM H
2
O
2
, no significant alteration in
Npun_R4582
relative mRNA levels was detected, while in cells treated with Co, Cu, Mn, Ni, or Zn and 60 μM peroxide, relative mRNA levels were generally above control or peroxide only treated cells. Disruption or overexpression of
npun_R4582
altered sensitivity to cells exposed to 60 μM H
2
O
2
and metals for treatments beyond the highest viable concentrations, or in a mixed metal solution for Npun_R4582
−
cells. Moreover, overexpression of
npun_R4582
increased cellular peroxidase activity in comparison with wild-type and Npun_R4582
−
cells, and reduced peroxide levels by over 50%. The addition of cobalt, manganese, nickel, and zinc increased the capacity of Npun_R4582 to reduce the rate or total levels of peroxide produced by cells growing under photooxidative conditions. The work presented confirms the function of NpunR4582 as a catalase and provides insights as to how cells reduce potentially lethal peroxide levels produced by photosynthesis. The findings also show how trace elements play crucial roles as enzymatic cofactors and how the role of Npun_R4582 in hydrogen peroxide breakdown is dependent on the type of metal and the level available to cells.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>28150026</pmid><doi>10.1007/s00253-017-8130-y</doi><tpages>20</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2017-05, Vol.101 (9), p.3781-3800 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_journals_1889306147 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Applied Microbial and Cell Physiology Astrobiology Bacteria Biomedical and Life Sciences Biotechnology Catalase - genetics Catalase - metabolism Catalysis Cobalt Coenzymes - metabolism Cyanobacteria Environmental science Enzymes Gene Deletion Gene Expression Gene Expression Profiling Hydrogen peroxide Investigations Life Sciences Manganese Metal concentrations Metals Metals - metabolism Microbial Genetics and Genomics Microbiology Nickel Nostoc - enzymology Nostoc - metabolism Oxidative stress Peroxides - metabolism Peroxides - toxicity Photosynthesis Real-Time Polymerase Chain Reaction RNA Studies Trace elements Zinc |
| title | Peroxide reduction by a metal-dependent catalase in Nostoc punctiforme (cyanobacteria) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T18%3A41%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Peroxide%20reduction%20by%20a%20metal-dependent%20catalase%20in%20Nostoc%20punctiforme%20(cyanobacteria)&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Hudek,%20L.&rft.date=2017-05-01&rft.volume=101&rft.issue=9&rft.spage=3781&rft.epage=3800&rft.pages=3781-3800&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-017-8130-y&rft_dat=%3Cgale_proqu%3EA550919033%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1889306147&rft_id=info:pmid/28150026&rft_galeid=A550919033&rfr_iscdi=true |