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
1 Citation (Scopus)


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.

Original languageEnglish
JournalHyperfine Interactions
Issue number1-4
Pages (from-to)69-73
Number of pages5
Publication statusPublished - 01.12.2000


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