Heterodisulfide reductase from Methanothermobacter marburgensis contains an active‐site [4Fe–4S] cluster that is directly involved in mediating heterodisulfide reduction
- 23 January 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 512 (1-3) , 263-268
- https://doi.org/10.1016/s0014-5793(02)02281-0
Abstract
Heterodisulfide reductases (HDRs) from methanogenic archaea are iron–sulfur flavoproteins or hemoproteins that catalyze the reversible reduction of the heterodisulfide (CoM-S–S-CoB) of the methanogenic thiol coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH). In this work, the ground- and excited-state electronic properties of the paramagnetic Fe–S clusters in Methanothermobacter marburgensis HDR have been characterized using the combination of electron paramagnetic resonance and variable-temperature magnetic circular dichroism spectroscopies. The results confirm multiple S=1/2 [4Fe–4S]+ clusters in dithionite-reduced HDR and reveal spectroscopically distinct S=1/2 [4Fe–4S]3+ clusters in oxidized HDR samples treated separately with the CoM-SH and CoB-SH cosubstrates. The active site of HDR is therefore shown to contain a [4Fe–4S] cluster that is directly involved in mediating heterodisulfide reduction. The catalytic mechanism of HDR is discussed in light of the crystallographic and spectroscopic studies of the related chloroplast ferredoxin:thioredoxin reductase class of disulfide reductases.Keywords
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