The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen
The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10...
Ausführliche Beschreibung
Gespeichert in:
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Bioenergetics - Amsterdam : Elsevier, 1188(1994), 3, Seite 205-212 |
| Übergeordnetes Werk: |
volume:1188 ; year:1994 ; number:3 ; pages:205-212 |
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| 520 | |a The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. | ||
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(DE-627)NLEJ185674216 (DE-599)GBVNLZ185674216 DE-627 ger DE-627 rakwb eng The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ribas-Carbo, M. oth Berry, J.A. oth Azcon-Bieto, J. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1188(1994), 3, Seite 205-212 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1188 year:1994 number:3 pages:205-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90037-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1188 1994 3 205-212 |
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(DE-627)NLEJ185674216 (DE-599)GBVNLZ185674216 DE-627 ger DE-627 rakwb eng The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ribas-Carbo, M. oth Berry, J.A. oth Azcon-Bieto, J. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1188(1994), 3, Seite 205-212 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1188 year:1994 number:3 pages:205-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90037-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1188 1994 3 205-212 |
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(DE-627)NLEJ185674216 (DE-599)GBVNLZ185674216 DE-627 ger DE-627 rakwb eng The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ribas-Carbo, M. oth Berry, J.A. oth Azcon-Bieto, J. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1188(1994), 3, Seite 205-212 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1188 year:1994 number:3 pages:205-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90037-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1188 1994 3 205-212 |
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(DE-627)NLEJ185674216 (DE-599)GBVNLZ185674216 DE-627 ger DE-627 rakwb eng The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ribas-Carbo, M. oth Berry, J.A. oth Azcon-Bieto, J. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1188(1994), 3, Seite 205-212 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1188 year:1994 number:3 pages:205-212 http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90037-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1188 1994 3 205-212 |
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The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen |
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The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. |
| abstractGer |
The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. |
| abstract_unstemmed |
The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration. |
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2024-07-06T04:38:58.907Z |
| _version_ |
1803803153038049280 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ185674216</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707023447.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185674216</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185674216</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="4"><subfield code="a">The reaction of the plant mitochondrial cyanide-resistant alternative oxidase with oxygen</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The dependence of electron flux through the cyanide-resistant respiratory pathway on the redox poise of the ubiquinone pool and oxygen concentration was studied in purified mitochondria isolated from green and etiolated soybean (Glycine max L. Merr. cv. Ransom) cotyledons at different ages (4 and 10 days after planting), soybean roots and mung bean (Vigna radiata L.R. Vilcz) hypocotyls. In soybean, the K"m of the alternative oxidase with respect to oxygen was found to vary between values of 10 and 20 μM. These are generally higher than values of the K"m for oxygen of the alternative oxidase reported previously (0.5 to 2.0 μM). In addition, the value of the K"m for oxygen varied with the redox poise of the ubiquinone pool, measured voltametrically; the more reduced the quinone pool, the larger the observed K"m. These results are at variance with the behavior expected of the kinetic model developed by Siedow and Moore (1993; Biochim. Biophys. Acta 1142, 165-174) which predicts that the K"m for oxygen should decrease as the quinone pool becomes more reduced. A modified kinetic model is developed that incorporates an additional reaction step involving activation of the four-electron reduced oxidase into the earlier kinetic model. The modified model successfully simulates the dependence of the alternative oxidase activity on both ubiquinone pool redox poise and oxygen concentration.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ribas-Carbo, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berry, J.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Azcon-Bieto, J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Siedow, J.N.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Bioenergetics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">1188(1994), 3, Seite 205-212</subfield><subfield code="w">(DE-627)NLEJ177198850</subfield><subfield code="w">(DE-600)2209370-9</subfield><subfield code="x">0005-2728</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1188</subfield><subfield code="g">year:1994</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:205-212</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2728(94)90037-X</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1188</subfield><subfield code="j">1994</subfield><subfield code="e">3</subfield><subfield code="h">205-212</subfield></datafield></record></collection>
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7.400672 |