Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-02

AUTHORS

Hirozo Oh-oka, Masayo Iwaki, Shigeru Itoh

ABSTRACT

The reaction between membrane-bound cytochrome c and the reaction center bacteriochlorophyll g dimer P798 was studied in the whole cells and isolated membranes of Heliobacterium gestii. In the whole cells, the flash-oxidized P798+ was rereduced in multiple exponential phases with half times (t1/2s) of 10 μs, 300 μs and 4 ms in relative amplitudes of 40, 35 and 25%, respectively. The faster two phases were in parallel with the oxidation of cytochrome c. In isolated membranes, a significantly slow oxidation of the membrane-bound cytochrome c was detected with t1/2 = 3 ms. This slow rate, however, again became faster with the addition of Mg2+. The rate showed a high temperature dependency giving apparent activation energies of 88.2 and 58.9 kJ/mol in the whole cells and isolated membranes, respectively. Therefore, membrane-bound cytochrome c donates electrons to the P798+ in a collisional reaction mode like the reaction of water-soluble proteins. The rereduction of the oxidized cytochrome c was suppressed by the addition of stigmatellin both in the whole cells and isolated membranes. This indicates that the electron transfer from the cytochrome bc complex to the photooxidized P798+ is mediated by the membrane-bound cytochrome c. The multiple flash excitation study showed that 2–3 hemes c were connected to the P798. By the heme staining after the SDS-PAGE analysis of the membraneous proteins, two cytochromes c were detected on the gel indicating apparent molecular masses of 17 and 30 kDa, respectively. The situation resembles the case in green sulfur bacteria, that is, the membrane-bound cyotochrome cz couples electron transfer between the cytochrome bc complex and the P840 reaction center complex. More... »

PAGES

137-147

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1014911832504

DOI

http://dx.doi.org/10.1023/a:1014911832504

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046605050

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16228507


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/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "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"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Department of Biology, Graduate School of Science, Osaka University, 560-0043, Osaka, Japan", 
          "id": "http://www.grid.ac/institutes/grid.136593.b", 
          "name": [
            "Department of Biology, Graduate School of Science, Osaka University, 560-0043, Osaka, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Oh-oka", 
        "givenName": "Hirozo", 
        "id": "sg:person.01270167323.88", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01270167323.88"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Basic Biology, 444-8585, Okazaki, Japan", 
          "id": "http://www.grid.ac/institutes/grid.419396.0", 
          "name": [
            "National Institute for Basic Biology, 444-8585, Okazaki, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Iwaki", 
        "givenName": "Masayo", 
        "id": "sg:person.01056504461.92", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01056504461.92"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Division of Material Science, Graduate School of Science, Nagoya University, 464-8602, Nagoya, Japan", 
          "id": "http://www.grid.ac/institutes/grid.27476.30", 
          "name": [
            "Division of Material Science, Graduate School of Science, Nagoya University, 464-8602, Nagoya, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Itoh", 
        "givenName": "Shigeru", 
        "id": "sg:person.012060635662.98", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.012060635662.98"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1007/bf00039173", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1005402640", 
          "https://doi.org/10.1007/bf00039173"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/0-306-47954-0_34", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1030117726", 
          "https://doi.org/10.1007/0-306-47954-0_34"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/0-306-47954-0_2", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1037370853", 
          "https://doi.org/10.1007/0-306-47954-0_2"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/978-94-009-0511-5_383", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1031718442", 
          "https://doi.org/10.1007/978-94-009-0511-5_383"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1007/0-306-47954-0_31", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1017725803", 
          "https://doi.org/10.1007/0-306-47954-0_31"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "2002-02", 
    "datePublishedReg": "2002-02-01", 
    "description": "The reaction between membrane-bound cytochrome c and the reaction center bacteriochlorophyll g dimer P798 was studied in the whole cells and isolated membranes of Heliobacterium gestii. In the whole cells, the flash-oxidized P798+ was rereduced in multiple exponential phases with half times (t1/2s) of 10 \u03bcs, 300 \u03bcs and 4 ms in relative amplitudes of 40, 35 and 25%, respectively. The faster two phases were in parallel with the oxidation of cytochrome c. In isolated membranes, a significantly slow oxidation of the membrane-bound cytochrome c was detected with t1/2 = 3 ms. This slow rate, however, again became faster with the addition of Mg2+. The rate showed a high temperature dependency giving apparent activation energies of 88.2 and 58.9 kJ/mol in the whole cells and isolated membranes, respectively. Therefore, membrane-bound cytochrome c donates electrons to the P798+ in a collisional reaction mode like the reaction of water-soluble proteins. The rereduction of the oxidized cytochrome c was suppressed by the addition of stigmatellin both in the whole cells and isolated membranes. This indicates that the electron transfer from the cytochrome bc complex to the photooxidized P798+ is mediated by the membrane-bound cytochrome c. The multiple flash excitation study showed that 2\u20133 hemes c were connected to the P798. By the heme staining after the SDS-PAGE analysis of the membraneous proteins, two cytochromes c were detected on the gel indicating apparent molecular masses of 17 and 30 kDa, respectively. The situation resembles the case in green sulfur bacteria, that is, the membrane-bound cyotochrome cz couples electron transfer between the cytochrome bc complex and the P840 reaction center complex.", 
    "genre": "article", 
    "id": "sg:pub.10.1023/a:1014911832504", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1022986", 
        "issn": [
          "0166-8595", 
          "1573-5079"
        ], 
        "name": "Photosynthesis Research", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "1-2", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "71"
      }
    ], 
    "keywords": [
      "membrane-bound cytochrome c", 
      "electron transfer", 
      "cytochrome bc complex", 
      "cytochrome c", 
      "reaction center bacteriochlorophyll", 
      "whole cells", 
      "Heliobacterium gestii", 
      "bc complex", 
      "P840-reaction center complex", 
      "reaction center complex", 
      "electron donation", 
      "photosynthetic reaction centers", 
      "P798", 
      "multiple exponential phases", 
      "oxidation", 
      "cytochrome c.", 
      "slow oxidation", 
      "addition of Mg2", 
      "apparent activation energy", 
      "activation energy", 
      "kJ/", 
      "reaction mode", 
      "water-soluble proteins", 
      "complexes", 
      "heme c", 
      "heme staining", 
      "SDS-PAGE analysis", 
      "apparent molecular mass", 
      "molecular mass", 
      "green sulfur bacteria", 
      "sulfur bacteria", 
      "center complex", 
      "reaction centers", 
      "reaction", 
      "cells", 
      "membrane", 
      "exponential phase", 
      "protein", 
      "excitation studies", 
      "membraneous proteins", 
      "bacteriochlorophyll", 
      "phase", 
      "\u03bcs", 
      "slower rate", 
      "Mg2", 
      "temperature dependency", 
      "electrons", 
      "rereduction", 
      "stigmatellin", 
      "transfer", 
      "gel", 
      "bacteria", 
      "C.", 
      "addition", 
      "energy", 
      "staining", 
      "half times", 
      "time", 
      "ms", 
      "parallel", 
      "t1/2", 
      "rate", 
      "mode", 
      "study", 
      "analysis", 
      "mass", 
      "Cz", 
      "donation", 
      "center", 
      "relative amplitude", 
      "amplitude", 
      "high temperature dependency", 
      "dependency", 
      "situation", 
      "cases"
    ], 
    "name": "Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii", 
    "pagination": "137-147", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1046605050"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1023/a:1014911832504"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "16228507"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1023/a:1014911832504", 
      "https://app.dimensions.ai/details/publication/pub.1046605050"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-08-04T16:54", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220804/entities/gbq_results/article/article_357.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1023/a:1014911832504"
  }
]
 

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.10.1023/a:1014911832504'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1023/a:1014911832504'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1023/a:1014911832504'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1023/a:1014911832504'


 

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

176 TRIPLES      21 PREDICATES      106 URIs      93 LITERALS      7 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1023/a:1014911832504 schema:about anzsrc-for:06
2 anzsrc-for:0601
3 schema:author N4790b0850b6944b0a6dd2aaf6e8fdd69
4 schema:citation sg:pub.10.1007/0-306-47954-0_2
5 sg:pub.10.1007/0-306-47954-0_31
6 sg:pub.10.1007/0-306-47954-0_34
7 sg:pub.10.1007/978-94-009-0511-5_383
8 sg:pub.10.1007/bf00039173
9 schema:datePublished 2002-02
10 schema:datePublishedReg 2002-02-01
11 schema:description The reaction between membrane-bound cytochrome c and the reaction center bacteriochlorophyll g dimer P798 was studied in the whole cells and isolated membranes of Heliobacterium gestii. In the whole cells, the flash-oxidized P798+ was rereduced in multiple exponential phases with half times (t1/2s) of 10 μs, 300 μs and 4 ms in relative amplitudes of 40, 35 and 25%, respectively. The faster two phases were in parallel with the oxidation of cytochrome c. In isolated membranes, a significantly slow oxidation of the membrane-bound cytochrome c was detected with t1/2 = 3 ms. This slow rate, however, again became faster with the addition of Mg2+. The rate showed a high temperature dependency giving apparent activation energies of 88.2 and 58.9 kJ/mol in the whole cells and isolated membranes, respectively. Therefore, membrane-bound cytochrome c donates electrons to the P798+ in a collisional reaction mode like the reaction of water-soluble proteins. The rereduction of the oxidized cytochrome c was suppressed by the addition of stigmatellin both in the whole cells and isolated membranes. This indicates that the electron transfer from the cytochrome bc complex to the photooxidized P798+ is mediated by the membrane-bound cytochrome c. The multiple flash excitation study showed that 2–3 hemes c were connected to the P798. By the heme staining after the SDS-PAGE analysis of the membraneous proteins, two cytochromes c were detected on the gel indicating apparent molecular masses of 17 and 30 kDa, respectively. The situation resembles the case in green sulfur bacteria, that is, the membrane-bound cyotochrome cz couples electron transfer between the cytochrome bc complex and the P840 reaction center complex.
12 schema:genre article
13 schema:isAccessibleForFree false
14 schema:isPartOf N2728dae74f784106b06c123d577c73ef
15 N7fb0efe75bc547fab80756fcce7bc00c
16 sg:journal.1022986
17 schema:keywords C.
18 Cz
19 Heliobacterium gestii
20 Mg2
21 P798
22 P840-reaction center complex
23 SDS-PAGE analysis
24 activation energy
25 addition
26 addition of Mg2
27 amplitude
28 analysis
29 apparent activation energy
30 apparent molecular mass
31 bacteria
32 bacteriochlorophyll
33 bc complex
34 cases
35 cells
36 center
37 center complex
38 complexes
39 cytochrome bc complex
40 cytochrome c
41 cytochrome c.
42 dependency
43 donation
44 electron donation
45 electron transfer
46 electrons
47 energy
48 excitation studies
49 exponential phase
50 gel
51 green sulfur bacteria
52 half times
53 heme c
54 heme staining
55 high temperature dependency
56 kJ/
57 mass
58 membrane
59 membrane-bound cytochrome c
60 membraneous proteins
61 mode
62 molecular mass
63 ms
64 multiple exponential phases
65 oxidation
66 parallel
67 phase
68 photosynthetic reaction centers
69 protein
70 rate
71 reaction
72 reaction center bacteriochlorophyll
73 reaction center complex
74 reaction centers
75 reaction mode
76 relative amplitude
77 rereduction
78 situation
79 slow oxidation
80 slower rate
81 staining
82 stigmatellin
83 study
84 sulfur bacteria
85 t1/2
86 temperature dependency
87 time
88 transfer
89 water-soluble proteins
90 whole cells
91 μs
92 schema:name Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii
93 schema:pagination 137-147
94 schema:productId N61f10d7315244ddbb25dda27ab86c119
95 N86d2c317ba9d4544bbb5563e17c8792d
96 N90b4d3ea9e464db4b13ae6b05fe7cec6
97 schema:sameAs https://app.dimensions.ai/details/publication/pub.1046605050
98 https://doi.org/10.1023/a:1014911832504
99 schema:sdDatePublished 2022-08-04T16:54
100 schema:sdLicense https://scigraph.springernature.com/explorer/license/
101 schema:sdPublisher Nc4b1487acf7b46068058c09313d8e3fc
102 schema:url https://doi.org/10.1023/a:1014911832504
103 sgo:license sg:explorer/license/
104 sgo:sdDataset articles
105 rdf:type schema:ScholarlyArticle
106 N2728dae74f784106b06c123d577c73ef schema:volumeNumber 71
107 rdf:type schema:PublicationVolume
108 N2de3dbf977654b0587f7108a56864964 rdf:first sg:person.012060635662.98
109 rdf:rest rdf:nil
110 N4790b0850b6944b0a6dd2aaf6e8fdd69 rdf:first sg:person.01270167323.88
111 rdf:rest N8b8194797fdd4a92b4dfe382e38ce926
112 N61f10d7315244ddbb25dda27ab86c119 schema:name dimensions_id
113 schema:value pub.1046605050
114 rdf:type schema:PropertyValue
115 N7fb0efe75bc547fab80756fcce7bc00c schema:issueNumber 1-2
116 rdf:type schema:PublicationIssue
117 N86d2c317ba9d4544bbb5563e17c8792d schema:name doi
118 schema:value 10.1023/a:1014911832504
119 rdf:type schema:PropertyValue
120 N8b8194797fdd4a92b4dfe382e38ce926 rdf:first sg:person.01056504461.92
121 rdf:rest N2de3dbf977654b0587f7108a56864964
122 N90b4d3ea9e464db4b13ae6b05fe7cec6 schema:name pubmed_id
123 schema:value 16228507
124 rdf:type schema:PropertyValue
125 Nc4b1487acf7b46068058c09313d8e3fc schema:name Springer Nature - SN SciGraph project
126 rdf:type schema:Organization
127 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
128 schema:name Biological Sciences
129 rdf:type schema:DefinedTerm
130 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
131 schema:name Biochemistry and Cell Biology
132 rdf:type schema:DefinedTerm
133 sg:journal.1022986 schema:issn 0166-8595
134 1573-5079
135 schema:name Photosynthesis Research
136 schema:publisher Springer Nature
137 rdf:type schema:Periodical
138 sg:person.01056504461.92 schema:affiliation grid-institutes:grid.419396.0
139 schema:familyName Iwaki
140 schema:givenName Masayo
141 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01056504461.92
142 rdf:type schema:Person
143 sg:person.012060635662.98 schema:affiliation grid-institutes:grid.27476.30
144 schema:familyName Itoh
145 schema:givenName Shigeru
146 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.012060635662.98
147 rdf:type schema:Person
148 sg:person.01270167323.88 schema:affiliation grid-institutes:grid.136593.b
149 schema:familyName Oh-oka
150 schema:givenName Hirozo
151 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01270167323.88
152 rdf:type schema:Person
153 sg:pub.10.1007/0-306-47954-0_2 schema:sameAs https://app.dimensions.ai/details/publication/pub.1037370853
154 https://doi.org/10.1007/0-306-47954-0_2
155 rdf:type schema:CreativeWork
156 sg:pub.10.1007/0-306-47954-0_31 schema:sameAs https://app.dimensions.ai/details/publication/pub.1017725803
157 https://doi.org/10.1007/0-306-47954-0_31
158 rdf:type schema:CreativeWork
159 sg:pub.10.1007/0-306-47954-0_34 schema:sameAs https://app.dimensions.ai/details/publication/pub.1030117726
160 https://doi.org/10.1007/0-306-47954-0_34
161 rdf:type schema:CreativeWork
162 sg:pub.10.1007/978-94-009-0511-5_383 schema:sameAs https://app.dimensions.ai/details/publication/pub.1031718442
163 https://doi.org/10.1007/978-94-009-0511-5_383
164 rdf:type schema:CreativeWork
165 sg:pub.10.1007/bf00039173 schema:sameAs https://app.dimensions.ai/details/publication/pub.1005402640
166 https://doi.org/10.1007/bf00039173
167 rdf:type schema:CreativeWork
168 grid-institutes:grid.136593.b schema:alternateName Department of Biology, Graduate School of Science, Osaka University, 560-0043, Osaka, Japan
169 schema:name Department of Biology, Graduate School of Science, Osaka University, 560-0043, Osaka, Japan
170 rdf:type schema:Organization
171 grid-institutes:grid.27476.30 schema:alternateName Division of Material Science, Graduate School of Science, Nagoya University, 464-8602, Nagoya, Japan
172 schema:name Division of Material Science, Graduate School of Science, Nagoya University, 464-8602, Nagoya, Japan
173 rdf:type schema:Organization
174 grid-institutes:grid.419396.0 schema:alternateName National Institute for Basic Biology, 444-8585, Okazaki, Japan
175 schema:name National Institute for Basic Biology, 444-8585, Okazaki, Japan
176 rdf:type schema:Organization
 




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


...