NADH-dependent metabolism of nitric oxide in alfalfa root cultures expressing barley hemoglobin
Transgenic alfalfa (Medicago sativa L.) root cultures expressing sense and antisense barley (Hordeum vulgare L.) hemoglobin were examined for their ability to metabolize NO. Extracts from lines overexpressing hemoglobin had approximately twice the NO conversion rate of either control or antisense li...
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| description | Transgenic alfalfa (Medicago sativa L.) root cultures expressing sense and antisense barley (Hordeum vulgare L.) hemoglobin were examined for their ability to metabolize NO. Extracts from lines overexpressing hemoglobin had approximately twice the NO conversion rate of either control or antisense lines under normoxic conditions. Only the control line showed a significant increase in the rate of NO degradation when placed under anaerobic conditions. The decline in NO was dependent on the presence of reduced pyridine nucleotide, with the NADH-dependent rate being about 2.5 times faster than the NADPH-dependent rate. Most of the activity was found in the cytosolic fraction of the extracts, while only small amounts were found in the cell wall, mitochondria, and 105,000-g membrane fraction. The NADH-dependent NO conversion exhibited a broad pH optimum in the range 7-8 and a strong affinity to NADH and NADPH (Km 3 micromolar for both). It was sensitive to diphenylene iodonium, an inhibitor of flavoproteins. The activity was strongly reduced by applying antibodies raised against recombinant barley hemoglobin. Extracts of Escherichia coli overexpressing barley hemoglobin showed a 4-fold higher rate of NO metabolism as compared to non-transformed cells. The NADH/NAD and NADPH/NADP ratios were higher in lines underexpressing hemoglobin, indicating that the presence of hemoglobin has an effect on these ratios. They were increased under hypoxia and antimycin A treatment. Alfalfa root extracts exhibited methemoglobin reductase activity, using either cytochrome c or recombinant barley hemoglobin as substrates. There was a correspondence between NO degradation and nitrate formation. The activity was eluted from a Superose 12 column as a single peak with molecular weight of 35±4 kDa, which corresponds to the size of the hemoglobin dimer. The results are consistent with an NO dioxygenase-like activity, with hemoglobin acting in concert with a flavoprotein, to metabolize NO to nitrate utilizing NADH as the electron donor. |
| doi_str_mv | 10.1007/s00425-003-1192-3 |
| format | Article |
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Extracts from lines overexpressing hemoglobin had approximately twice the NO conversion rate of either control or antisense lines under normoxic conditions. Only the control line showed a significant increase in the rate of NO degradation when placed under anaerobic conditions. The decline in NO was dependent on the presence of reduced pyridine nucleotide, with the NADH-dependent rate being about 2.5 times faster than the NADPH-dependent rate. Most of the activity was found in the cytosolic fraction of the extracts, while only small amounts were found in the cell wall, mitochondria, and 105,000-g membrane fraction. The NADH-dependent NO conversion exhibited a broad pH optimum in the range 7-8 and a strong affinity to NADH and NADPH (Km 3 micromolar for both). It was sensitive to diphenylene iodonium, an inhibitor of flavoproteins. The activity was strongly reduced by applying antibodies raised against recombinant barley hemoglobin. Extracts of Escherichia coli overexpressing barley hemoglobin showed a 4-fold higher rate of NO metabolism as compared to non-transformed cells. The NADH/NAD and NADPH/NADP ratios were higher in lines underexpressing hemoglobin, indicating that the presence of hemoglobin has an effect on these ratios. They were increased under hypoxia and antimycin A treatment. Alfalfa root extracts exhibited methemoglobin reductase activity, using either cytochrome c or recombinant barley hemoglobin as substrates. There was a correspondence between NO degradation and nitrate formation. The activity was eluted from a Superose 12 column as a single peak with molecular weight of 35±4 kDa, which corresponds to the size of the hemoglobin dimer. The results are consistent with an NO dioxygenase-like activity, with hemoglobin acting in concert with a flavoprotein, to metabolize NO to nitrate utilizing NADH as the electron donor.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-003-1192-3</identifier><identifier>PMID: 14740214</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin: Springer-Verlag</publisher><subject>Alfalfa ; Anaerobic conditions ; Bacteria ; Barley ; Biological and medical sciences ; Cell Hypoxia ; Cells, Cultured ; Cytochrome-B Reductase - metabolism ; Dehydrogenases ; E coli ; Enzymes ; forage crops ; Fundamental and applied biological sciences. Psychology ; gene overexpression ; Hemeproteins - metabolism ; Hemoglobins ; Hordeum vulgare ; Hydrogen-Ion Concentration ; Hypoxia ; malate dehydrogenase ; Malate Dehydrogenase - metabolism ; Medicago sativa ; Medicago sativa - genetics ; Medicago sativa - metabolism ; Metabolism ; methemoglobin reductase ; Molecular weight ; NAD (coenzyme) ; NAD - metabolism ; NADP (coenzyme) ; Nitrates ; Nitric oxide ; Nitric Oxide - metabolism ; Oxides ; Oxygen ; Oxygen - metabolism ; Photosynthesis, respiration. Anabolism, catabolism ; plant extracts ; plant hemoglobin-like protein ; Plant physiology and development ; Plant Proteins ; Plant Roots - metabolism ; Plants ; Plants, Genetically Modified ; Pyridine nucleotides ; Pyridines - metabolism ; roots ; tissue culture ; transgenes ; transgenic plants</subject><ispartof>Planta, 2004-05, Vol.219 (1), p.95-102</ispartof><rights>Springer-Verlag Berlin Heidelberg 2004</rights><rights>2004 INIST-CNRS</rights><rights>Springer-Verlag 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-dda70f6091672d18c59ea3a214b2ca1b02a328bd86298003388d55f857fdccd93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23388409$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23388409$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15701409$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14740214$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Igamberdiev, A.U</creatorcontrib><creatorcontrib>Seregelyes, C</creatorcontrib><creatorcontrib>Manac'h, N</creatorcontrib><creatorcontrib>Hill, R.D</creatorcontrib><title>NADH-dependent metabolism of nitric oxide in alfalfa root cultures expressing barley hemoglobin</title><title>Planta</title><addtitle>Planta</addtitle><description>Transgenic alfalfa (Medicago sativa L.) root cultures expressing sense and antisense barley (Hordeum vulgare L.) hemoglobin were examined for their ability to metabolize NO. Extracts from lines overexpressing hemoglobin had approximately twice the NO conversion rate of either control or antisense lines under normoxic conditions. Only the control line showed a significant increase in the rate of NO degradation when placed under anaerobic conditions. The decline in NO was dependent on the presence of reduced pyridine nucleotide, with the NADH-dependent rate being about 2.5 times faster than the NADPH-dependent rate. Most of the activity was found in the cytosolic fraction of the extracts, while only small amounts were found in the cell wall, mitochondria, and 105,000-g membrane fraction. The NADH-dependent NO conversion exhibited a broad pH optimum in the range 7-8 and a strong affinity to NADH and NADPH (Km 3 micromolar for both). It was sensitive to diphenylene iodonium, an inhibitor of flavoproteins. The activity was strongly reduced by applying antibodies raised against recombinant barley hemoglobin. Extracts of Escherichia coli overexpressing barley hemoglobin showed a 4-fold higher rate of NO metabolism as compared to non-transformed cells. The NADH/NAD and NADPH/NADP ratios were higher in lines underexpressing hemoglobin, indicating that the presence of hemoglobin has an effect on these ratios. They were increased under hypoxia and antimycin A treatment. Alfalfa root extracts exhibited methemoglobin reductase activity, using either cytochrome c or recombinant barley hemoglobin as substrates. There was a correspondence between NO degradation and nitrate formation. The activity was eluted from a Superose 12 column as a single peak with molecular weight of 35±4 kDa, which corresponds to the size of the hemoglobin dimer. The results are consistent with an NO dioxygenase-like activity, with hemoglobin acting in concert with a flavoprotein, to metabolize NO to nitrate utilizing NADH as the electron donor.</description><subject>Alfalfa</subject><subject>Anaerobic conditions</subject><subject>Bacteria</subject><subject>Barley</subject><subject>Biological and medical sciences</subject><subject>Cell Hypoxia</subject><subject>Cells, Cultured</subject><subject>Cytochrome-B Reductase - metabolism</subject><subject>Dehydrogenases</subject><subject>E coli</subject><subject>Enzymes</subject><subject>forage crops</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene overexpression</subject><subject>Hemeproteins - metabolism</subject><subject>Hemoglobins</subject><subject>Hordeum vulgare</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hypoxia</subject><subject>malate dehydrogenase</subject><subject>Malate Dehydrogenase - metabolism</subject><subject>Medicago sativa</subject><subject>Medicago sativa - genetics</subject><subject>Medicago sativa - metabolism</subject><subject>Metabolism</subject><subject>methemoglobin reductase</subject><subject>Molecular weight</subject><subject>NAD (coenzyme)</subject><subject>NAD - metabolism</subject><subject>NADP (coenzyme)</subject><subject>Nitrates</subject><subject>Nitric oxide</subject><subject>Nitric Oxide - metabolism</subject><subject>Oxides</subject><subject>Oxygen</subject><subject>Oxygen - metabolism</subject><subject>Photosynthesis, respiration. Anabolism, catabolism</subject><subject>plant extracts</subject><subject>plant hemoglobin-like protein</subject><subject>Plant physiology and development</subject><subject>Plant Proteins</subject><subject>Plant Roots - metabolism</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Pyridine nucleotides</subject><subject>Pyridines - metabolism</subject><subject>roots</subject><subject>tissue culture</subject><subject>transgenes</subject><subject>transgenic plants</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</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>eNpdkU9v1DAQxS0EokvhA3AALKRyM4z_JLaPVaEUqYID9Gw5trN4lcSLnUjtt8dRVlRCsjSH95vnmTcIvabwkQLITwVAsIYAcEKpZoQ_QTsqOCMMhHqKdlVgBDRvztCLUg4AVZTyOTqjQgpgVOyQ-X75-Yb4cAyTD9OMxzDbLg2xjDj1eIpzjg6n--gDjhO2Q78-nFOasVuGecmh4HB_rKXEaY87m4fwgH-HMe2H1MXpJXpWW0p4darn6O76y6-rG3L74-u3q8tb4kTbzsR7K6FvQdNWMk-Va3Sw3NYRO-Ys7YBZzlTnVcu0qmtxpXzT9KqRvXfOa36OPmy-x5z-LKHMZozFhWGwU0hLMZJqYLIVFXz_H3hIS57qbEYxUK3UdHWjG-RyKiWH3hxzHG1-MBTMGr3Zojd1FLNGb3jteXsyXrox-MeOU9YVuDgBtrgaY7aTi-WRa2S9D6yfv9m4Q5lT_qezdelNf7fpvU3G7nP1uPvJgHKoomi15n8B8_yeDg</recordid><startdate>20040501</startdate><enddate>20040501</enddate><creator>Igamberdiev, A.U</creator><creator>Seregelyes, C</creator><creator>Manac'h, N</creator><creator>Hill, R.D</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040501</creationdate><title>NADH-dependent metabolism of nitric oxide in alfalfa root cultures expressing barley hemoglobin</title><author>Igamberdiev, A.U ; Seregelyes, C ; Manac'h, N ; Hill, R.D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466t-dda70f6091672d18c59ea3a214b2ca1b02a328bd86298003388d55f857fdccd93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Alfalfa</topic><topic>Anaerobic conditions</topic><topic>Bacteria</topic><topic>Barley</topic><topic>Biological and medical sciences</topic><topic>Cell Hypoxia</topic><topic>Cells, Cultured</topic><topic>Cytochrome-B Reductase - metabolism</topic><topic>Dehydrogenases</topic><topic>E coli</topic><topic>Enzymes</topic><topic>forage crops</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene overexpression</topic><topic>Hemeproteins - metabolism</topic><topic>Hemoglobins</topic><topic>Hordeum vulgare</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hypoxia</topic><topic>malate dehydrogenase</topic><topic>Malate Dehydrogenase - metabolism</topic><topic>Medicago sativa</topic><topic>Medicago sativa - genetics</topic><topic>Medicago sativa - metabolism</topic><topic>Metabolism</topic><topic>methemoglobin reductase</topic><topic>Molecular weight</topic><topic>NAD (coenzyme)</topic><topic>NAD - metabolism</topic><topic>NADP (coenzyme)</topic><topic>Nitrates</topic><topic>Nitric oxide</topic><topic>Nitric Oxide - metabolism</topic><topic>Oxides</topic><topic>Oxygen</topic><topic>Oxygen - metabolism</topic><topic>Photosynthesis, respiration. Anabolism, catabolism</topic><topic>plant extracts</topic><topic>plant hemoglobin-like protein</topic><topic>Plant physiology and development</topic><topic>Plant Proteins</topic><topic>Plant Roots - metabolism</topic><topic>Plants</topic><topic>Plants, Genetically Modified</topic><topic>Pyridine nucleotides</topic><topic>Pyridines - metabolism</topic><topic>roots</topic><topic>tissue culture</topic><topic>transgenes</topic><topic>transgenic plants</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Igamberdiev, A.U</creatorcontrib><creatorcontrib>Seregelyes, C</creatorcontrib><creatorcontrib>Manac'h, N</creatorcontrib><creatorcontrib>Hill, R.D</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Igamberdiev, A.U</au><au>Seregelyes, C</au><au>Manac'h, N</au><au>Hill, R.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NADH-dependent metabolism of nitric oxide in alfalfa root cultures expressing barley hemoglobin</atitle><jtitle>Planta</jtitle><addtitle>Planta</addtitle><date>2004-05-01</date><risdate>2004</risdate><volume>219</volume><issue>1</issue><spage>95</spage><epage>102</epage><pages>95-102</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>Transgenic alfalfa (Medicago sativa L.) root cultures expressing sense and antisense barley (Hordeum vulgare L.) hemoglobin were examined for their ability to metabolize NO. Extracts from lines overexpressing hemoglobin had approximately twice the NO conversion rate of either control or antisense lines under normoxic conditions. Only the control line showed a significant increase in the rate of NO degradation when placed under anaerobic conditions. The decline in NO was dependent on the presence of reduced pyridine nucleotide, with the NADH-dependent rate being about 2.5 times faster than the NADPH-dependent rate. Most of the activity was found in the cytosolic fraction of the extracts, while only small amounts were found in the cell wall, mitochondria, and 105,000-g membrane fraction. The NADH-dependent NO conversion exhibited a broad pH optimum in the range 7-8 and a strong affinity to NADH and NADPH (Km 3 micromolar for both). It was sensitive to diphenylene iodonium, an inhibitor of flavoproteins. The activity was strongly reduced by applying antibodies raised against recombinant barley hemoglobin. Extracts of Escherichia coli overexpressing barley hemoglobin showed a 4-fold higher rate of NO metabolism as compared to non-transformed cells. The NADH/NAD and NADPH/NADP ratios were higher in lines underexpressing hemoglobin, indicating that the presence of hemoglobin has an effect on these ratios. They were increased under hypoxia and antimycin A treatment. Alfalfa root extracts exhibited methemoglobin reductase activity, using either cytochrome c or recombinant barley hemoglobin as substrates. There was a correspondence between NO degradation and nitrate formation. The activity was eluted from a Superose 12 column as a single peak with molecular weight of 35±4 kDa, which corresponds to the size of the hemoglobin dimer. The results are consistent with an NO dioxygenase-like activity, with hemoglobin acting in concert with a flavoprotein, to metabolize NO to nitrate utilizing NADH as the electron donor.</abstract><cop>Berlin</cop><pub>Springer-Verlag</pub><pmid>14740214</pmid><doi>10.1007/s00425-003-1192-3</doi><tpages>8</tpages></addata></record> |
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| subjects | Alfalfa Anaerobic conditions Bacteria Barley Biological and medical sciences Cell Hypoxia Cells, Cultured Cytochrome-B Reductase - metabolism Dehydrogenases E coli Enzymes forage crops Fundamental and applied biological sciences. Psychology gene overexpression Hemeproteins - metabolism Hemoglobins Hordeum vulgare Hydrogen-Ion Concentration Hypoxia malate dehydrogenase Malate Dehydrogenase - metabolism Medicago sativa Medicago sativa - genetics Medicago sativa - metabolism Metabolism methemoglobin reductase Molecular weight NAD (coenzyme) NAD - metabolism NADP (coenzyme) Nitrates Nitric oxide Nitric Oxide - metabolism Oxides Oxygen Oxygen - metabolism Photosynthesis, respiration. Anabolism, catabolism plant extracts plant hemoglobin-like protein Plant physiology and development Plant Proteins Plant Roots - metabolism Plants Plants, Genetically Modified Pyridine nucleotides Pyridines - metabolism roots tissue culture transgenes transgenic plants |
| title | NADH-dependent metabolism of nitric oxide in alfalfa root cultures expressing barley hemoglobin |
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