A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae

Po-Chi Lin; Andrea Puhar; Karin Türk; Stergios Piligkos; Eckhard Bill; Frank Neese; Julia Steuber

doi:10.1074/jbc.C500171200

A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae

Po-Chi Lin
, Andrea Puhar
, Karin Türk
, Stergios Piligkos
, Eckhard Bill
, Frank Neese
, Julia Steuber^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

11 Downloads (Pure)

Abstract

The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae contains a single Fe-S cluster localized in subunit NqrF. Here we study the electronic properties of the Fe-S center in a truncated version of the NqrF subunit comprising only its ferredoxin-like Fe-S domain. Mössbauer spectroscopy of the Fe-S domain in the oxidized state is consistent with a binuclear Fe-S cluster with tetrahedral sulfur coordination by the cysteine residues Cys(70), Cys(76), Cys(79), and Cys(111). Important sequence motifs surrounding these cysteines are conserved in the Fe-S domain and in vertebrate-type ferredoxins. The magnetic circular dichroism spectra of the photochemically reduced Fe-S domain exhibit a striking similarity to the magnetic circular dichroism spectra of vertebrate-type ferredoxins required for the in vivo assembly of iron-sulfur clusters. This study reveals a novel function for vertebrate-type [2Fe-2S] clusters as redox cofactors in respiratory dehydrogenases.

Original language	English
Pages (from-to)	22560-22563
Number of pages	4
Journal	The Journal of Biological Chemistry
Volume	280
Issue number	24
Early online date	03 May 2005
DOIs	https://doi.org/10.1074/jbc.C500171200
Publication status	Published - 17 Jun 2005
Externally published	Yes

Keywords

Amino Acid Motifs
Amino Acid Sequence
Animals
Catalysis
Circular Dichroism
Cysteine/chemistry
Ferredoxins/chemistry
Iron-Sulfur Proteins/chemistry
Magnetics
Molecular Sequence Data
Oxidation-Reduction
Oxygen Consumption
Protein Structure, Tertiary
Quinone Reductases/chemistry
Sequence Homology, Amino Acid
Sodium/chemistry
Sodium-Potassium-Exchanging ATPase/chemistry
Spectroscopy, Mossbauer/methods
Ultraviolet Rays
Vertebrates
Vibrio cholerae/enzymology

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10.1074/jbc.C500171200Licence: CC BY

A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae
Copyright 2005 the authors. This is an open access article published under a Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Final published version, 635 KBLicence: CC BY

Cite this

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title = "A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae",

abstract = "The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae contains a single Fe-S cluster localized in subunit NqrF. Here we study the electronic properties of the Fe-S center in a truncated version of the NqrF subunit comprising only its ferredoxin-like Fe-S domain. M{\"o}ssbauer spectroscopy of the Fe-S domain in the oxidized state is consistent with a binuclear Fe-S cluster with tetrahedral sulfur coordination by the cysteine residues Cys(70), Cys(76), Cys(79), and Cys(111). Important sequence motifs surrounding these cysteines are conserved in the Fe-S domain and in vertebrate-type ferredoxins. The magnetic circular dichroism spectra of the photochemically reduced Fe-S domain exhibit a striking similarity to the magnetic circular dichroism spectra of vertebrate-type ferredoxins required for the in vivo assembly of iron-sulfur clusters. This study reveals a novel function for vertebrate-type [2Fe-2S] clusters as redox cofactors in respiratory dehydrogenases.",

keywords = "Amino Acid Motifs, Amino Acid Sequence, Animals, Catalysis, Circular Dichroism, Cysteine/chemistry, Ferredoxins/chemistry, Iron-Sulfur Proteins/chemistry, Magnetics, Molecular Sequence Data, Oxidation-Reduction, Oxygen Consumption, Protein Structure, Tertiary, Quinone Reductases/chemistry, Sequence Homology, Amino Acid, Sodium/chemistry, Sodium-Potassium-Exchanging ATPase/chemistry, Spectroscopy, Mossbauer/methods, Ultraviolet Rays, Vertebrates, Vibrio cholerae/enzymology",

author = "Po-Chi Lin and Andrea Puhar and Karin T{\"u}rk and Stergios Piligkos and Eckhard Bill and Frank Neese and Julia Steuber",

year = "2005",

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doi = "10.1074/jbc.C500171200",

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T1 - A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae

AU - Lin, Po-Chi

AU - Puhar, Andrea

AU - Türk, Karin

AU - Piligkos, Stergios

AU - Bill, Eckhard

AU - Neese, Frank

AU - Steuber, Julia

PY - 2005/6/17

Y1 - 2005/6/17

N2 - The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae contains a single Fe-S cluster localized in subunit NqrF. Here we study the electronic properties of the Fe-S center in a truncated version of the NqrF subunit comprising only its ferredoxin-like Fe-S domain. Mössbauer spectroscopy of the Fe-S domain in the oxidized state is consistent with a binuclear Fe-S cluster with tetrahedral sulfur coordination by the cysteine residues Cys(70), Cys(76), Cys(79), and Cys(111). Important sequence motifs surrounding these cysteines are conserved in the Fe-S domain and in vertebrate-type ferredoxins. The magnetic circular dichroism spectra of the photochemically reduced Fe-S domain exhibit a striking similarity to the magnetic circular dichroism spectra of vertebrate-type ferredoxins required for the in vivo assembly of iron-sulfur clusters. This study reveals a novel function for vertebrate-type [2Fe-2S] clusters as redox cofactors in respiratory dehydrogenases.

AB - The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae contains a single Fe-S cluster localized in subunit NqrF. Here we study the electronic properties of the Fe-S center in a truncated version of the NqrF subunit comprising only its ferredoxin-like Fe-S domain. Mössbauer spectroscopy of the Fe-S domain in the oxidized state is consistent with a binuclear Fe-S cluster with tetrahedral sulfur coordination by the cysteine residues Cys(70), Cys(76), Cys(79), and Cys(111). Important sequence motifs surrounding these cysteines are conserved in the Fe-S domain and in vertebrate-type ferredoxins. The magnetic circular dichroism spectra of the photochemically reduced Fe-S domain exhibit a striking similarity to the magnetic circular dichroism spectra of vertebrate-type ferredoxins required for the in vivo assembly of iron-sulfur clusters. This study reveals a novel function for vertebrate-type [2Fe-2S] clusters as redox cofactors in respiratory dehydrogenases.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Animals

KW - Catalysis

KW - Circular Dichroism

KW - Cysteine/chemistry

KW - Ferredoxins/chemistry

KW - Iron-Sulfur Proteins/chemistry

KW - Magnetics

KW - Molecular Sequence Data

KW - Oxidation-Reduction

KW - Oxygen Consumption

KW - Protein Structure, Tertiary

KW - Quinone Reductases/chemistry

KW - Sequence Homology, Amino Acid

KW - Sodium/chemistry

KW - Sodium-Potassium-Exchanging ATPase/chemistry

KW - Spectroscopy, Mossbauer/methods

KW - Ultraviolet Rays

KW - Vertebrates

KW - Vibrio cholerae/enzymology

U2 - 10.1074/jbc.C500171200

DO - 10.1074/jbc.C500171200

M3 - Article

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SN - 0021-9258

VL - 280

SP - 22560

EP - 22563

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

IS - 24

ER -

A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae

Abstract

Keywords

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