Properties of the Tight Nucleotide Binding Site of Chloroplast Coupling Factor CF1 Deficient in δ- and ε-Subunits View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1998

AUTHORS

O. I. Vitseva , A. N. Malyan

ABSTRACT

The chloroplast coupling factor (CF1) is the soluble part of the H+-ATPase (ATP synthase) complex which is responsible for phosphorylation of ADP coupled with transmembrane proton translocation. CF1 contains six nucleotide binding sites, three of which are catalytic (1). These sites are located on three pairs of α/β subunits which together with the γ-subunit form the smalest possible complex preserving catalitic properties of intact CF1. One of the catalitic sites binds tightly ADP (2). However, it can exchange with ADP or ATP in the medium. We used this reaction to determine affinity of sites for nucleotides. To avoid nucleotide interaction with other binding sites, the ATP(ADP)/CF1 ratios are kept substoichiometric. Experiments on CF1 showed that the tightly bound ATP/ADP ratio and relative site affinity for the nucleotides are strongly dependent on medium pH (3). This suggests that the properties of the tight nucleotide binding site are controlled by the state of specific protonated groups of the enzyme. The question arises whether the minor subunits contribute to pH-dependent changes in site affinity for the nucleotides, and where exactly the groups are located. To answer it, we studied the kinetics of the interaction of ATP and ADP with the tight nucleotides binding site of CF1 deficient in the δ- and ε-subunits at two pH values: 6.0 and 8.0. More... »

PAGES

1723-1726

Book

TITLE

Photosynthesis: Mechanisms and Effects

ISBN

978-0-7923-5547-2
978-94-011-3953-3

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_403

DOI

http://dx.doi.org/10.1007/978-94-011-3953-3_403

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090937454


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Russian Academy of Sciences", 
          "id": "https://www.grid.ac/institutes/grid.4886.2", 
          "name": [
            "Russian Academy of Science"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Vitseva", 
        "givenName": "O. I.", 
        "id": "sg:person.0673461777.21", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0673461777.21"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Russian Academy of Sciences", 
          "id": "https://www.grid.ac/institutes/grid.4886.2", 
          "name": [
            "Russian Academy of Science"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Malyan", 
        "givenName": "A. N.", 
        "id": "sg:person.01353143155.16", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01353143155.16"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "https://doi.org/10.1016/0005-2728(85)90167-7", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1009268650"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0005-2728(85)90167-7", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1009268650"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/bf00051731", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1020939536", 
          "https://doi.org/10.1007/bf00051731"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/bf00051731", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1020939536", 
          "https://doi.org/10.1007/bf00051731"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0003-2697(76)90527-3", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1025529346"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0005-2728(93)90063-l", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1025949432"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0005-2728(93)90063-l", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1025949432"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/bi00525a003", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1055179437"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://app.dimensions.ai/details/publication/pub.1081751706", 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1998", 
    "datePublishedReg": "1998-01-01", 
    "description": "The chloroplast coupling factor (CF1) is the soluble part of the H+-ATPase (ATP synthase) complex which is responsible for phosphorylation of ADP coupled with transmembrane proton translocation. CF1 contains six nucleotide binding sites, three of which are catalytic (1). These sites are located on three pairs of \u03b1/\u03b2 subunits which together with the \u03b3-subunit form the smalest possible complex preserving catalitic properties of intact CF1. One of the catalitic sites binds tightly ADP (2). However, it can exchange with ADP or ATP in the medium. We used this reaction to determine affinity of sites for nucleotides. To avoid nucleotide interaction with other binding sites, the ATP(ADP)/CF1 ratios are kept substoichiometric. Experiments on CF1 showed that the tightly bound ATP/ADP ratio and relative site affinity for the nucleotides are strongly dependent on medium pH (3). This suggests that the properties of the tight nucleotide binding site are controlled by the state of specific protonated groups of the enzyme. The question arises whether the minor subunits contribute to pH-dependent changes in site affinity for the nucleotides, and where exactly the groups are located. To answer it, we studied the kinetics of the interaction of ATP and ADP with the tight nucleotides binding site of CF1 deficient in the \u03b4- and \u03b5-subunits at two pH values: 6.0 and 8.0.", 
    "editor": [
      {
        "familyName": "Garab", 
        "givenName": "G.", 
        "type": "Person"
      }
    ], 
    "genre": "chapter", 
    "id": "sg:pub.10.1007/978-94-011-3953-3_403", 
    "inLanguage": [
      "en"
    ], 
    "isAccessibleForFree": false, 
    "isPartOf": {
      "isbn": [
        "978-0-7923-5547-2", 
        "978-94-011-3953-3"
      ], 
      "name": "Photosynthesis: Mechanisms and Effects", 
      "type": "Book"
    }, 
    "name": "Properties of the Tight Nucleotide Binding Site of Chloroplast Coupling Factor CF1 Deficient in \u03b4- and \u03b5-Subunits", 
    "pagination": "1723-1726", 
    "productId": [
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/978-94-011-3953-3_403"
        ]
      }, 
      {
        "name": "readcube_id", 
        "type": "PropertyValue", 
        "value": [
          "d7ba0a401542dd8dfaa0d60398c57e3e37a6250254263a576ed6df76daa0bff9"
        ]
      }, 
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1090937454"
        ]
      }
    ], 
    "publisher": {
      "location": "Dordrecht", 
      "name": "Springer Netherlands", 
      "type": "Organisation"
    }, 
    "sameAs": [
      "https://doi.org/10.1007/978-94-011-3953-3_403", 
      "https://app.dimensions.ai/details/publication/pub.1090937454"
    ], 
    "sdDataset": "chapters", 
    "sdDatePublished": "2019-04-15T12:36", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8663_00000279.jsonl", 
    "type": "Chapter", 
    "url": "http://link.springer.com/10.1007/978-94-011-3953-3_403"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_403'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_403'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_403'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-3953-3_403'


 

This table displays all metadata directly associated to this object as RDF triples.

90 TRIPLES      23 PREDICATES      33 URIs      20 LITERALS      8 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/978-94-011-3953-3_403 schema:about anzsrc-for:06
2 anzsrc-for:0601
3 schema:author Ncf86fdddf014457685842aadf5a815cc
4 schema:citation sg:pub.10.1007/bf00051731
5 https://app.dimensions.ai/details/publication/pub.1081751706
6 https://doi.org/10.1016/0003-2697(76)90527-3
7 https://doi.org/10.1016/0005-2728(85)90167-7
8 https://doi.org/10.1016/0005-2728(93)90063-l
9 https://doi.org/10.1021/bi00525a003
10 schema:datePublished 1998
11 schema:datePublishedReg 1998-01-01
12 schema:description The chloroplast coupling factor (CF1) is the soluble part of the H+-ATPase (ATP synthase) complex which is responsible for phosphorylation of ADP coupled with transmembrane proton translocation. CF1 contains six nucleotide binding sites, three of which are catalytic (1). These sites are located on three pairs of α/β subunits which together with the γ-subunit form the smalest possible complex preserving catalitic properties of intact CF1. One of the catalitic sites binds tightly ADP (2). However, it can exchange with ADP or ATP in the medium. We used this reaction to determine affinity of sites for nucleotides. To avoid nucleotide interaction with other binding sites, the ATP(ADP)/CF1 ratios are kept substoichiometric. Experiments on CF1 showed that the tightly bound ATP/ADP ratio and relative site affinity for the nucleotides are strongly dependent on medium pH (3). This suggests that the properties of the tight nucleotide binding site are controlled by the state of specific protonated groups of the enzyme. The question arises whether the minor subunits contribute to pH-dependent changes in site affinity for the nucleotides, and where exactly the groups are located. To answer it, we studied the kinetics of the interaction of ATP and ADP with the tight nucleotides binding site of CF1 deficient in the δ- and ε-subunits at two pH values: 6.0 and 8.0.
13 schema:editor Nc440c643a07f4f99a3a8202922b40c44
14 schema:genre chapter
15 schema:inLanguage en
16 schema:isAccessibleForFree false
17 schema:isPartOf Na60f6d66f57340309a6ed6d34934a819
18 schema:name Properties of the Tight Nucleotide Binding Site of Chloroplast Coupling Factor CF1 Deficient in δ- and ε-Subunits
19 schema:pagination 1723-1726
20 schema:productId N1165ff44c0b2426f9b28fe9eb7ca1a4d
21 Nb3d531f09550457ea21aa66bb75e16ab
22 Ne36c3410111e442c85a90eccfecf7273
23 schema:publisher N9100490715db46648b6891b51f61c9b2
24 schema:sameAs https://app.dimensions.ai/details/publication/pub.1090937454
25 https://doi.org/10.1007/978-94-011-3953-3_403
26 schema:sdDatePublished 2019-04-15T12:36
27 schema:sdLicense https://scigraph.springernature.com/explorer/license/
28 schema:sdPublisher N5f0105f18c7b4aa79951d1d6f1bb8830
29 schema:url http://link.springer.com/10.1007/978-94-011-3953-3_403
30 sgo:license sg:explorer/license/
31 sgo:sdDataset chapters
32 rdf:type schema:Chapter
33 N1165ff44c0b2426f9b28fe9eb7ca1a4d schema:name doi
34 schema:value 10.1007/978-94-011-3953-3_403
35 rdf:type schema:PropertyValue
36 N5f0105f18c7b4aa79951d1d6f1bb8830 schema:name Springer Nature - SN SciGraph project
37 rdf:type schema:Organization
38 N9100490715db46648b6891b51f61c9b2 schema:location Dordrecht
39 schema:name Springer Netherlands
40 rdf:type schema:Organisation
41 Na60f6d66f57340309a6ed6d34934a819 schema:isbn 978-0-7923-5547-2
42 978-94-011-3953-3
43 schema:name Photosynthesis: Mechanisms and Effects
44 rdf:type schema:Book
45 Nb3d531f09550457ea21aa66bb75e16ab schema:name readcube_id
46 schema:value d7ba0a401542dd8dfaa0d60398c57e3e37a6250254263a576ed6df76daa0bff9
47 rdf:type schema:PropertyValue
48 Nbcf55bbebe8643ada0631e7221ff8e36 rdf:first sg:person.01353143155.16
49 rdf:rest rdf:nil
50 Nc0d40d27b28c4c1e9da0a213282a7e0a schema:familyName Garab
51 schema:givenName G.
52 rdf:type schema:Person
53 Nc440c643a07f4f99a3a8202922b40c44 rdf:first Nc0d40d27b28c4c1e9da0a213282a7e0a
54 rdf:rest rdf:nil
55 Ncf86fdddf014457685842aadf5a815cc rdf:first sg:person.0673461777.21
56 rdf:rest Nbcf55bbebe8643ada0631e7221ff8e36
57 Ne36c3410111e442c85a90eccfecf7273 schema:name dimensions_id
58 schema:value pub.1090937454
59 rdf:type schema:PropertyValue
60 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
61 schema:name Biological Sciences
62 rdf:type schema:DefinedTerm
63 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
64 schema:name Biochemistry and Cell Biology
65 rdf:type schema:DefinedTerm
66 sg:person.01353143155.16 schema:affiliation https://www.grid.ac/institutes/grid.4886.2
67 schema:familyName Malyan
68 schema:givenName A. N.
69 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01353143155.16
70 rdf:type schema:Person
71 sg:person.0673461777.21 schema:affiliation https://www.grid.ac/institutes/grid.4886.2
72 schema:familyName Vitseva
73 schema:givenName O. I.
74 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0673461777.21
75 rdf:type schema:Person
76 sg:pub.10.1007/bf00051731 schema:sameAs https://app.dimensions.ai/details/publication/pub.1020939536
77 https://doi.org/10.1007/bf00051731
78 rdf:type schema:CreativeWork
79 https://app.dimensions.ai/details/publication/pub.1081751706 schema:CreativeWork
80 https://doi.org/10.1016/0003-2697(76)90527-3 schema:sameAs https://app.dimensions.ai/details/publication/pub.1025529346
81 rdf:type schema:CreativeWork
82 https://doi.org/10.1016/0005-2728(85)90167-7 schema:sameAs https://app.dimensions.ai/details/publication/pub.1009268650
83 rdf:type schema:CreativeWork
84 https://doi.org/10.1016/0005-2728(93)90063-l schema:sameAs https://app.dimensions.ai/details/publication/pub.1025949432
85 rdf:type schema:CreativeWork
86 https://doi.org/10.1021/bi00525a003 schema:sameAs https://app.dimensions.ai/details/publication/pub.1055179437
87 rdf:type schema:CreativeWork
88 https://www.grid.ac/institutes/grid.4886.2 schema:alternateName Russian Academy of Sciences
89 schema:name Russian Academy of Science
90 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...