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          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents

ID: 680391.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Advanced electron paramagnetic resonance on the catalytic iron–sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate: quinone reductase
Authors:Fielding, Alistair J.; Parey, Kristian; Ermler, Ulrich; Scheller, Silvan; Jaun, Bernhard; Bennati, Marina
Date of Publication (YYYY-MM-DD):2013-12
Title of Journal:Journal of Biological Inorganic Chemistry
Journal Abbrev.:J. Biol. Inorg. Chem.
Issue / Number:8
Start Page:905
End Page:915
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Heterodisulfide reductase (Hdr) is a key enzyme in the energy metabolism of methanogenic archaea. The enzyme catalyzes the reversible reduction of the heterodisulfide (CoM-S-S-CoB) to the thiol coenzymesM(CoM-SH) and B (CoB-SH). Cleavage of CoM-S-S-CoB at an unusual FeS cluster reveals unique substrate chemistry. The cluster is fixed by cysteines of two cysteine-rich CCG domain sequence motifs (CX31–39CCX35–36CXXC) of subunit HdrB of the Methanothermobacter marburgensis HdrABC complex. We report on Q-band (34 GHz) 57Fe electron-nuclear double resonance (ENDOR) spectroscopic measurements on the oxidized form of the cluster found in HdrABC and in two other CCG-domain-containing proteins, recombinant HdrB of Hdr from M. marburgensis and recombinant SdhE of succinate: quinone reductase from Sulfolobus solfataricus P2. The spectra at 34 GHz show clearly improved resolution arising from the absence of proton resonances and polarization effects. Systematic spectral simulations of 34 GHz data combined with previous 9 GHz data allowed the unambiguous assignment of four 57Fe hyperfine couplings to the cluster in all three proteins. 13C Mims ENDOR spectra of labelled CoM-SH were consistent with the attachment of the substrate to the cluster in HdrABC, whereas in the other two proteins no substrate is present. 57Fe resonances in all three systems revealed unusually large 57Fe ENDOR hyperfine splitting as compared to known systems. The results infer that the cluster’s unique magnetic properties arise from the CCG binding motif.
Free Keywords:ENDOR; Iron–sulfur cluster; Heterodisulfide reductase; EPR
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
MPI für biophysikalische Chemie/AG Marina Bennati
External Affiliations:Laboratory of Organic Chemistry, ETH-Zurich, 8093 Zurich, Switzerland;
Department of Chemistry, Georg-August University, Göttingen, Germany
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