Photoreduction of the Non Heme Iron in Photosystem II Studied by FTIR Difference Spectroscopy View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1993

AUTHORS

Rainer Hienerwadel , Alain Boussac , Catherine Berthomieu

ABSTRACT

In photosystem II (PS II) as in the bacterial photosynthetic reaction center (RC), two quinones QA and QB constitute the primary and secondary electron acceptors. The three-dimensional structure of the bacterial RC showed that a non-heme iron (Fe) is located between QA and QB. This Fe is liganded to four histidine residues, the side-chain of a glutamate residue provides the fifth and sixth ligands (1). In PS II, the Fe is conserved and four histidine residues of the apoprotein could constitute its ligands. There is no equivalent in PS II of the glutamate present in the bacterial RC. A number of experiments showed that a bicarbonate ion interacts with the protein in the surounding of Fe and could possibly be a Fe ligand (2). This bicarbonate can be extracted or exchanged by formate; this procedure affects electron transfer between QA and QB (3). In PS II, the Fe can be oxidized by ferricyanide (4). In this study, we aimed to determine and characterize the Fe ligands in PS II by light-induced FTIR difference spectroscopy. Therefore, we monitored the photoreduction of Fe in PS II preparations where it is oxidized by ferricyanide in the dark. We used PS II membranes trypsinized at pH 6.2 where a very large fraction of Fe is accessible to ferricyanide. In the FTIR difference spectrum, we can follow the changes of interaction between Fe and the protein moeity (notably histidine residues) as well as IR signals from the bicarbonate ion. More... »

PAGES

317-318

Book

TITLE

Fifth International Conference on the Spectroscopy of Biological Molecules

ISBN

978-94-010-4855-2
978-94-011-1934-4

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-1934-4_118

DOI

http://dx.doi.org/10.1007/978-94-011-1934-4_118

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036772780


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/2008/02", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Physical Sciences", 
        "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"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0299", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Other Physical 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": "Institut f\u00fcr Biophysik, Albertstr. 23, W-79104, Freiburg, Germany", 
          "id": "http://www.grid.ac/institutes/None", 
          "name": [
            "Institut f\u00fcr Biophysik, Albertstr. 23, W-79104, Freiburg, Germany"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Hienerwadel", 
        "givenName": "Rainer", 
        "id": "sg:person.01072334743.16", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01072334743.16"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.457334.2", 
          "name": [
            "SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Boussac", 
        "givenName": "Alain", 
        "id": "sg:person.01232306506.30", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01232306506.30"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France", 
          "id": "http://www.grid.ac/institutes/grid.457334.2", 
          "name": [
            "SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Berthomieu", 
        "givenName": "Catherine", 
        "id": "sg:person.0641716334.91", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0641716334.91"
        ], 
        "type": "Person"
      }
    ], 
    "datePublished": "1993", 
    "datePublishedReg": "1993-01-01", 
    "description": "In photosystem II (PS II) as in the bacterial photosynthetic reaction center (RC), two quinones QA and QB constitute the primary and secondary electron acceptors. The three-dimensional structure of the bacterial RC showed that a non-heme iron (Fe) is located between QA and QB. This Fe is liganded to four histidine residues, the side-chain of a glutamate residue provides the fifth and sixth ligands (1). In PS II, the Fe is conserved and four histidine residues of the apoprotein could constitute its ligands. There is no equivalent in PS II of the glutamate present in the bacterial RC. A number of experiments showed that a bicarbonate ion interacts with the protein in the surounding of Fe and could possibly be a Fe ligand (2). This bicarbonate can be extracted or exchanged by formate; this procedure affects electron transfer between QA and QB (3). In PS II, the Fe can be oxidized by ferricyanide (4). In this study, we aimed to determine and characterize the Fe ligands in PS II by light-induced FTIR difference spectroscopy. Therefore, we monitored the photoreduction of Fe in PS II preparations where it is oxidized by ferricyanide in the dark. We used PS II membranes trypsinized at pH 6.2 where a very large fraction of Fe is accessible to ferricyanide. In the FTIR difference spectrum, we can follow the changes of interaction between Fe and the protein moeity (notably histidine residues) as well as IR signals from the bicarbonate ion.", 
    "editor": [
      {
        "familyName": "Theophanides", 
        "givenName": "Theophile", 
        "type": "Person"
      }, 
      {
        "familyName": "Anastassopoulou", 
        "givenName": "Jane", 
        "type": "Person"
      }, 
      {
        "familyName": "Fotopoulos", 
        "givenName": "Nikolaos", 
        "type": "Person"
      }
    ], 
    "genre": "chapter", 
    "id": "sg:pub.10.1007/978-94-011-1934-4_118", 
    "isAccessibleForFree": false, 
    "isPartOf": {
      "isbn": [
        "978-94-010-4855-2", 
        "978-94-011-1934-4"
      ], 
      "name": "Fifth International Conference on the Spectroscopy of Biological Molecules", 
      "type": "Book"
    }, 
    "keywords": [
      "FTIR difference spectroscopy", 
      "bacterial reaction centers", 
      "reaction centers", 
      "non-heme iron", 
      "PS II", 
      "Fe ligands", 
      "light-induced FTIR difference spectroscopy", 
      "difference spectroscopy", 
      "photosystem II", 
      "histidine residues", 
      "bacterial photosynthetic reaction centers", 
      "FTIR difference spectra", 
      "PS II preparations", 
      "PS II membranes", 
      "secondary electron acceptor", 
      "photosynthetic reaction centers", 
      "electron transfer", 
      "sixth ligand", 
      "ion interacts", 
      "quinone QA", 
      "three-dimensional structure", 
      "electron acceptor", 
      "glutamate residues", 
      "ligands", 
      "heme iron", 
      "IR signals", 
      "bicarbonate ions", 
      "photoreduction", 
      "spectroscopy", 
      "difference spectra", 
      "ferricyanide", 
      "Fe", 
      "large fraction", 
      "residues", 
      "change of interaction", 
      "QB", 
      "pH 6.2", 
      "iron", 
      "number of experiments", 
      "acceptor", 
      "ions", 
      "moeity", 
      "formate", 
      "spectra", 
      "protein", 
      "preparation", 
      "QA", 
      "interacts", 
      "protein moeity", 
      "apoprotein", 
      "membrane", 
      "structure", 
      "transfer", 
      "dark", 
      "glutamate", 
      "interaction", 
      "signals", 
      "bicarbonate", 
      "experiments", 
      "equivalent", 
      "fraction", 
      "changes", 
      "center", 
      "number", 
      "study", 
      "procedure"
    ], 
    "name": "Photoreduction of the Non Heme Iron in Photosystem II Studied by FTIR Difference Spectroscopy", 
    "pagination": "317-318", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1036772780"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/978-94-011-1934-4_118"
        ]
      }
    ], 
    "publisher": {
      "name": "Springer Nature", 
      "type": "Organisation"
    }, 
    "sameAs": [
      "https://doi.org/10.1007/978-94-011-1934-4_118", 
      "https://app.dimensions.ai/details/publication/pub.1036772780"
    ], 
    "sdDataset": "chapters", 
    "sdDatePublished": "2022-09-02T16:17", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220902/entities/gbq_results/chapter/chapter_396.jsonl", 
    "type": "Chapter", 
    "url": "https://doi.org/10.1007/978-94-011-1934-4_118"
  }
]
 

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.10.1007/978-94-011-1934-4_118'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-1934-4_118'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-1934-4_118'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/978-94-011-1934-4_118'


 

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

160 TRIPLES      22 PREDICATES      93 URIs      84 LITERALS      7 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/978-94-011-1934-4_118 schema:about anzsrc-for:02
2 anzsrc-for:0299
3 anzsrc-for:06
4 anzsrc-for:0601
5 schema:author N1482f6936ba946d2a5943590f6eff7d4
6 schema:datePublished 1993
7 schema:datePublishedReg 1993-01-01
8 schema:description In photosystem II (PS II) as in the bacterial photosynthetic reaction center (RC), two quinones QA and QB constitute the primary and secondary electron acceptors. The three-dimensional structure of the bacterial RC showed that a non-heme iron (Fe) is located between QA and QB. This Fe is liganded to four histidine residues, the side-chain of a glutamate residue provides the fifth and sixth ligands (1). In PS II, the Fe is conserved and four histidine residues of the apoprotein could constitute its ligands. There is no equivalent in PS II of the glutamate present in the bacterial RC. A number of experiments showed that a bicarbonate ion interacts with the protein in the surounding of Fe and could possibly be a Fe ligand (2). This bicarbonate can be extracted or exchanged by formate; this procedure affects electron transfer between QA and QB (3). In PS II, the Fe can be oxidized by ferricyanide (4). In this study, we aimed to determine and characterize the Fe ligands in PS II by light-induced FTIR difference spectroscopy. Therefore, we monitored the photoreduction of Fe in PS II preparations where it is oxidized by ferricyanide in the dark. We used PS II membranes trypsinized at pH 6.2 where a very large fraction of Fe is accessible to ferricyanide. In the FTIR difference spectrum, we can follow the changes of interaction between Fe and the protein moeity (notably histidine residues) as well as IR signals from the bicarbonate ion.
9 schema:editor Ndfa5e79018464bedbe40bd1291874c5a
10 schema:genre chapter
11 schema:isAccessibleForFree false
12 schema:isPartOf N485303c2aae04f45a2b1a2e3f2aadeb7
13 schema:keywords FTIR difference spectra
14 FTIR difference spectroscopy
15 Fe
16 Fe ligands
17 IR signals
18 PS II
19 PS II membranes
20 PS II preparations
21 QA
22 QB
23 acceptor
24 apoprotein
25 bacterial photosynthetic reaction centers
26 bacterial reaction centers
27 bicarbonate
28 bicarbonate ions
29 center
30 change of interaction
31 changes
32 dark
33 difference spectra
34 difference spectroscopy
35 electron acceptor
36 electron transfer
37 equivalent
38 experiments
39 ferricyanide
40 formate
41 fraction
42 glutamate
43 glutamate residues
44 heme iron
45 histidine residues
46 interaction
47 interacts
48 ion interacts
49 ions
50 iron
51 large fraction
52 ligands
53 light-induced FTIR difference spectroscopy
54 membrane
55 moeity
56 non-heme iron
57 number
58 number of experiments
59 pH 6.2
60 photoreduction
61 photosynthetic reaction centers
62 photosystem II
63 preparation
64 procedure
65 protein
66 protein moeity
67 quinone QA
68 reaction centers
69 residues
70 secondary electron acceptor
71 signals
72 sixth ligand
73 spectra
74 spectroscopy
75 structure
76 study
77 three-dimensional structure
78 transfer
79 schema:name Photoreduction of the Non Heme Iron in Photosystem II Studied by FTIR Difference Spectroscopy
80 schema:pagination 317-318
81 schema:productId N043aedd1a673455583302bf65770fde6
82 N0ac609ef32bd4947bc7f1116b908dc4f
83 schema:publisher Nbaf87c1ad3c149afa93a785951d561f1
84 schema:sameAs https://app.dimensions.ai/details/publication/pub.1036772780
85 https://doi.org/10.1007/978-94-011-1934-4_118
86 schema:sdDatePublished 2022-09-02T16:17
87 schema:sdLicense https://scigraph.springernature.com/explorer/license/
88 schema:sdPublisher N716569ea8a8445bead587119d58a1930
89 schema:url https://doi.org/10.1007/978-94-011-1934-4_118
90 sgo:license sg:explorer/license/
91 sgo:sdDataset chapters
92 rdf:type schema:Chapter
93 N043aedd1a673455583302bf65770fde6 schema:name doi
94 schema:value 10.1007/978-94-011-1934-4_118
95 rdf:type schema:PropertyValue
96 N0ac609ef32bd4947bc7f1116b908dc4f schema:name dimensions_id
97 schema:value pub.1036772780
98 rdf:type schema:PropertyValue
99 N1482f6936ba946d2a5943590f6eff7d4 rdf:first sg:person.01072334743.16
100 rdf:rest N3d0d4ab08c414903b8163b988ceb3c38
101 N23636a1509924d938349817624db0f4c rdf:first Nef315e9439854ab094ea38a181912a09
102 rdf:rest N9d8ac68c1c6b4c00abe93124c14a18fa
103 N3d0d4ab08c414903b8163b988ceb3c38 rdf:first sg:person.01232306506.30
104 rdf:rest Nef05b1a6ce24491daeb0b3063a9b7d53
105 N458bd9bcfe6f4b58b0c60ce62ea8f8bd schema:familyName Fotopoulos
106 schema:givenName Nikolaos
107 rdf:type schema:Person
108 N485303c2aae04f45a2b1a2e3f2aadeb7 schema:isbn 978-94-010-4855-2
109 978-94-011-1934-4
110 schema:name Fifth International Conference on the Spectroscopy of Biological Molecules
111 rdf:type schema:Book
112 N716569ea8a8445bead587119d58a1930 schema:name Springer Nature - SN SciGraph project
113 rdf:type schema:Organization
114 N9d8ac68c1c6b4c00abe93124c14a18fa rdf:first N458bd9bcfe6f4b58b0c60ce62ea8f8bd
115 rdf:rest rdf:nil
116 Nbaf87c1ad3c149afa93a785951d561f1 schema:name Springer Nature
117 rdf:type schema:Organisation
118 Nd9218c16198c4167a4eed3e6cb8f4da1 schema:familyName Theophanides
119 schema:givenName Theophile
120 rdf:type schema:Person
121 Ndfa5e79018464bedbe40bd1291874c5a rdf:first Nd9218c16198c4167a4eed3e6cb8f4da1
122 rdf:rest N23636a1509924d938349817624db0f4c
123 Nef05b1a6ce24491daeb0b3063a9b7d53 rdf:first sg:person.0641716334.91
124 rdf:rest rdf:nil
125 Nef315e9439854ab094ea38a181912a09 schema:familyName Anastassopoulou
126 schema:givenName Jane
127 rdf:type schema:Person
128 anzsrc-for:02 schema:inDefinedTermSet anzsrc-for:
129 schema:name Physical Sciences
130 rdf:type schema:DefinedTerm
131 anzsrc-for:0299 schema:inDefinedTermSet anzsrc-for:
132 schema:name Other Physical Sciences
133 rdf:type schema:DefinedTerm
134 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
135 schema:name Biological Sciences
136 rdf:type schema:DefinedTerm
137 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
138 schema:name Biochemistry and Cell Biology
139 rdf:type schema:DefinedTerm
140 sg:person.01072334743.16 schema:affiliation grid-institutes:None
141 schema:familyName Hienerwadel
142 schema:givenName Rainer
143 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01072334743.16
144 rdf:type schema:Person
145 sg:person.01232306506.30 schema:affiliation grid-institutes:grid.457334.2
146 schema:familyName Boussac
147 schema:givenName Alain
148 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01232306506.30
149 rdf:type schema:Person
150 sg:person.0641716334.91 schema:affiliation grid-institutes:grid.457334.2
151 schema:familyName Berthomieu
152 schema:givenName Catherine
153 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0641716334.91
154 rdf:type schema:Person
155 grid-institutes:None schema:alternateName Institut für Biophysik, Albertstr. 23, W-79104, Freiburg, Germany
156 schema:name Institut für Biophysik, Albertstr. 23, W-79104, Freiburg, Germany
157 rdf:type schema:Organization
158 grid-institutes:grid.457334.2 schema:alternateName SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France
159 schema:name SBE/DBCM, CEN Saclay, 91 191, Gif-sur-Yvette Cedex, France
160 rdf:type schema:Organization
 




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


...