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• W2051503192 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." @default.
• W2051503192 created "2016-06-24" @default.
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• W2051503192 date "2002-01-23" @default.
• W2051503192 modified "2023-10-17" @default.
• W2051503192 title "Heterodisulfide reductase from <i>Methanothermobacter marburgensis</i> contains an active‐site [4Fe–4S] cluster that is directly involved in mediating heterodisulfide reduction" @default.
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• W2051503192 doi "https://doi.org/10.1016/s0014-5793(02)02281-0" @default.
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