Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria
A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in dark...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Nyrén, Pål [verfasserIn] Strid, Åke [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1991 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 77(1991), 2/3, Seite 0 |
| Übergeordnetes Werk: |
volume:77 ; year:1991 ; number:2/3 ; pages:0 |
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| DOI / URN: |
10.1111/j.1574-6968.1991.tb04359.x |
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NLEJ239732588 |
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| 520 | |a A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. | ||
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10.1111/j.1574-6968.1991.tb04359.x doi (DE-627)NLEJ239732588 DE-627 ger DE-627 rakwb Nyrén, Pål verfasserin aut Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Bacterial bioenergetics Strid, Åke verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04359.x doi (DE-627)NLEJ239732588 DE-627 ger DE-627 rakwb Nyrén, Pål verfasserin aut Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Bacterial bioenergetics Strid, Åke verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04359.x doi (DE-627)NLEJ239732588 DE-627 ger DE-627 rakwb Nyrén, Pål verfasserin aut Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Bacterial bioenergetics Strid, Åke verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04359.x doi (DE-627)NLEJ239732588 DE-627 ger DE-627 rakwb Nyrén, Pål verfasserin aut Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Bacterial bioenergetics Strid, Åke verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04359.x doi (DE-627)NLEJ239732588 DE-627 ger DE-627 rakwb Nyrén, Pål verfasserin aut Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Bacterial bioenergetics Strid, Åke verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. |
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A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. |
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A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge. |
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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">NLEJ239732588</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707093423.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1991 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1574-6968.1991.tb04359.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ239732588</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="100" ind1="1" ind2=" "><subfield code="a">Nyrén, Pål</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase in some phototrophic bacteria</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1991</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward. The main task for this enzyme is to maintain a substantial protonmotive force under circumstances of lower energy, e.g. in darkness. Granules containing pyrophosphate (PPi) are proposed to be the source of hydrolyzable free PPi. Under conditions of ample energy, for instance in high light, the H+-PPase, together with other PPi-producing enzymes in the cell, provide PPi for re-formation of the phosphate-containing granules, i.e. the H+-PPase is a PPi synthesizer during illumination. The hypothesis is discussed in connection with present knowledge.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bacterial bioenergetics</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Strid, Åke</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="a">Federation of European Microbiological Societies ; GKD-ID: 114439X</subfield><subfield code="t">FEMS microbiology letters</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">77(1991), 2/3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927053</subfield><subfield code="w">(DE-600)1501716-3</subfield><subfield code="x">1574-6968</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:77</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:2/3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1574-6968.1991.tb04359.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</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">77</subfield><subfield code="j">1991</subfield><subfield code="e">2/3</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.399288 |