Glutamate 94 of [2Fe2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803 (Q58480364)

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scientific article published on 01 November 1996

Language	Label	Description	Also known as
English	Glutamate 94 of [2Fe2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803	scientific article published on 01 November 1996

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scholarly article

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21 October 2019

Glutamate 94 of [2Fe-2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803 (English)

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21 October 2019

Francisco Navarro

2

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21 October 2019

Francisco J. Florencio

4

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21 October 2019

author name string

S Schmitz

1

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21 October 2019

C K Kutzki

3

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21 October 2019

H Böhme

5

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21 October 2019

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1 November 1996

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21 October 2019

Biochimica et Biophysica Acta

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21 October 2019

1277

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21 October 2019

1-2

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21 October 2019

135-140

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21 October 2019

Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii.

1 reference

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Oxidation-reduction properties of the ferredoxin-linked glutamate synthase from spinach leaf

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Purification and characterization of the ferredoxin-glutamate synthase from the unicellular cyanobacterium Synechococcus sp. PCC 6301

1 reference

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7 January 2021

Existence of two ferredoxin-glutamate synthases in the cyanobacterium Synechocystis sp. PCC 6803. Isolation and insertional inactivation of gltB and gltS genes

1 reference

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7 January 2021

Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis

1 reference

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7 January 2021

Transient kinetic and oxidation-reduction studies of spinach ferredoxin:nitrite oxidoreductase

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7 January 2021

Ferredoxin-dependent chloroplast enzymes

1 reference

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7 January 2021

Further characterization by site-directed mutagenesis of the protein-protein interface in the ferredoxin/ferredoxin:NADP+ reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2896%2900095-3

7 January 2021

Antigenic similarities between ferredoxin-dependent nitrite reductase and glutamate synthase fromChlamydomonas reinhardtii

1 reference

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7 January 2021

Modification of arginyl residues in ferredoxin-NADP reductase from spinach leaves

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7 January 2021

Arginyl groups involved in the binding of Anabaena ferredoxin--NADP+ reductase to NADP+ and to ferredoxin

1 reference

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7 January 2021

Lysine residues on ferredoxin-NADP+ reductase from Anabaena sp. PCC 7119 involved in substrate binding

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Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Ammonia assimilating enzymes from cyanobacteria: In situ and in vitro assay using high-performance liquid chromatography

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7 January 2021

Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119

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Expression of Anabaena ferredoxin genes in Escherichia coli

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7 January 2021

Binding of ferredoxin to ferredoxin:NADP+ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment

1 reference

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7 January 2021

Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties

1 reference

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7 January 2021

Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2896%2900095-3

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0005-2728(96)00095-3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8950376%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8950376%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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