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 Fe2.5+Fe2.5+ (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 | |
Publication status | Published - 01.12.2000 |