Iron sulfur clusters in benzoyl-CoA reductase

C. Meier; V. Schünemann; A. X. Trautwein; G. Fuchs; D. Lowe; M. Boll

doi:10.1023/A:1012684426401

Iron sulfur clusters in benzoyl-CoA reductase

C. Meier^*, V. Schünemann, A. X. Trautwein, G. Fuchs, D. Lowe, M. Boll

^*Corresponding author for this work

Institute of Physics

1 Citation (Scopus)

Abstract

The enzyme benzoyl-CoA reductase (BCR) has been studied by Mössbauer spectroscopy in fields up to 7 T and at temperature down to 4.2 K. It has been shown that the oxidized BCR contains three diamagnetic [4Fe-4S]²⁺ centers. Treatment of BCR with dithionite or deazaflavin reduces only one of the three centers from [4Fe-4S]²⁺ to [4Fe-4S]¹⁺. The latter exhibits Mössbauer spectra at 4.2 K in applied fields characteristic for Fe^2.5+Fe^2.5+ (S = 9/2) and Fe²⁺Fe²⁺ (S = 4) pairs, both coupled antiferromagnetically to total spin S = 1/2.

Original language	English
Journal	Hyperfine Interactions
Volume	126
Issue number	1-4
Pages (from-to)	69-73
Number of pages	5
ISSN	0304-3843
DOIs	https://doi.org/10.1023/A:1012684426401
Publication status	Published - 01.12.2000

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title = "Iron sulfur clusters in benzoyl-CoA reductase",

abstract = "The enzyme benzoyl-CoA reductase (BCR) has been studied by M{\"o}ssbauer spectroscopy in fields up to 7 T and at temperature down to 4.2 K. It has been shown that the oxidized BCR contains three diamagnetic [4Fe-4S]2+ centers. Treatment of BCR with dithionite or deazaflavin reduces only one of the three centers from [4Fe-4S]2+ to [4Fe-4S]1+. The latter exhibits M{\"o}ssbauer spectra at 4.2 K in applied fields characteristic for Fe2.5+Fe2.5+ (S = 9/2) and Fe2+Fe2+ (S = 4) pairs, both coupled antiferromagnetically to total spin S = 1/2.",

author = "C. Meier and V. Sch{\"u}nemann and Trautwein, {A. X.} and G. Fuchs and D. Lowe and M. Boll",

year = "2000",

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doi = "10.1023/A:1012684426401",

language = "English",

volume = "126",

pages = "69--73",

journal = "Hyperfine Interactions",

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TY - JOUR

T1 - Iron sulfur clusters in benzoyl-CoA reductase

AU - Meier, C.

AU - Schünemann, V.

AU - Trautwein, A. X.

AU - Fuchs, G.

AU - Lowe, D.

AU - Boll, M.

PY - 2000/12/1

Y1 - 2000/12/1

N2 - The enzyme benzoyl-CoA reductase (BCR) has been studied by Mössbauer spectroscopy in fields up to 7 T and at temperature down to 4.2 K. It has been shown that the oxidized BCR contains three diamagnetic [4Fe-4S]2+ centers. Treatment of BCR with dithionite or deazaflavin reduces only one of the three centers from [4Fe-4S]2+ to [4Fe-4S]1+. The latter exhibits Mössbauer spectra at 4.2 K in applied fields characteristic for Fe2.5+Fe2.5+ (S = 9/2) and Fe2+Fe2+ (S = 4) pairs, both coupled antiferromagnetically to total spin S = 1/2.

AB - The enzyme benzoyl-CoA reductase (BCR) has been studied by Mössbauer spectroscopy in fields up to 7 T and at temperature down to 4.2 K. It has been shown that the oxidized BCR contains three diamagnetic [4Fe-4S]2+ centers. Treatment of BCR with dithionite or deazaflavin reduces only one of the three centers from [4Fe-4S]2+ to [4Fe-4S]1+. The latter exhibits Mössbauer spectra at 4.2 K in applied fields characteristic for Fe2.5+Fe2.5+ (S = 9/2) and Fe2+Fe2+ (S = 4) pairs, both coupled antiferromagnetically to total spin S = 1/2.

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U2 - 10.1023/A:1012684426401

DO - 10.1023/A:1012684426401

M3 - Journal articles

AN - SCOPUS:0034454118

SN - 0304-3843

VL - 126

SP - 69

EP - 73

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Iron sulfur clusters in benzoyl-CoA reductase

Abstract

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