The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria
In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1991 |
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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, 1059(1991), 2, Seite 121-140 |
| Übergeordnetes Werk: |
volume:1059 ; year:1991 ; number:2 ; pages:121-140 |
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NLEJ185333478 |
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| 245 | 1 | 4 | |a The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria |
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| 520 | |a In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. | ||
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(DE-627)NLEJ185333478 (DE-599)GBVNLZ185333478 DE-627 ger DE-627 rakwb eng The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moore, A.L. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1059(1991), 2, Seite 121-140 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1059 year:1991 number:2 pages:121-140 http://dx.doi.org/10.1016/S0005-2728(05)80197-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1059 1991 2 121-140 |
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(DE-627)NLEJ185333478 (DE-599)GBVNLZ185333478 DE-627 ger DE-627 rakwb eng The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moore, A.L. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1059(1991), 2, Seite 121-140 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1059 year:1991 number:2 pages:121-140 http://dx.doi.org/10.1016/S0005-2728(05)80197-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1059 1991 2 121-140 |
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(DE-627)NLEJ185333478 (DE-599)GBVNLZ185333478 DE-627 ger DE-627 rakwb eng The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moore, A.L. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1059(1991), 2, Seite 121-140 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1059 year:1991 number:2 pages:121-140 http://dx.doi.org/10.1016/S0005-2728(05)80197-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1059 1991 2 121-140 |
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(DE-627)NLEJ185333478 (DE-599)GBVNLZ185333478 DE-627 ger DE-627 rakwb eng The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moore, A.L. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1059(1991), 2, Seite 121-140 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1059 year:1991 number:2 pages:121-140 http://dx.doi.org/10.1016/S0005-2728(05)80197-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1059 1991 2 121-140 |
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(DE-627)NLEJ185333478 (DE-599)GBVNLZ185333478 DE-627 ger DE-627 rakwb eng The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moore, A.L. oth Siedow, J.N. oth in Biochimica et Biophysica Acta (BBA)/Bioenergetics Amsterdam : Elsevier 1059(1991), 2, Seite 121-140 (DE-627)NLEJ177198850 (DE-600)2209370-9 0005-2728 nnns volume:1059 year:1991 number:2 pages:121-140 http://dx.doi.org/10.1016/S0005-2728(05)80197-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1059 1991 2 121-140 |
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The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria |
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In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. |
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In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. |
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In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase. |
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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">NLEJ185333478</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707013902.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1991 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185333478</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185333478</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 regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1991</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">In addition to possessing multiple NAD(P)H dehydrogenases, most plant mitochondria contain a cyanide- and antimycin-insensitive alternative terminal oxidase. Although the general characterisics of this terminal oxidase have been known for a considerable number of years, the mechanism by which it is regulated is unclear and until recently there has been relatively little information on its exact nature. In the past 5 years, however, the application of molecular and novel voltametric techniques has advanced our understanding of this oxidase considerably. In this article, we review briefly current understanding on the structure and function of the multiple NADH dehydrogenases and consider, in detail, the nature and regulation of the alternative oxidase. We derive a kinetic model for electron transfer through the ubiquinone pool based on a proposed model for the reduction of the oxidase by quinol and show how this can account for deviations from Q-pool behaviour. We review information on the attempts to isolate and characterise the oxidase and finally consider the molecular aspects of the expression of the alternative oxidase.</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">Moore, A.L.</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">1059(1991), 2, Seite 121-140</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:1059</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:121-140</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/S0005-2728(05)80197-5</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">1059</subfield><subfield code="j">1991</subfield><subfield code="e">2</subfield><subfield code="h">121-140</subfield></datafield></record></collection>
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7.399583 |