Abstract
TlpA and ScoI of Bradyrhizobium japonicum are membrane-anchored thioredoxin-like proteins oriented towards the periplasm. TlpA is a protein-disulfide reductase. ScoI is a copper chaperone for cytochrome oxidase biogenesis. TlpA with its negative redox potential (Eo′ −256mV) was shown here to reduce oxidized ScoI, for which we determined a less negative Eo′ (−160mV). The fast forward reaction (rate constant 9.4×104M−1s−1) was typical for physiologically relevant disulfide exchange reactions. A transient TlpA-ScoI heterodisulfide formed between Cys107 of TlpA’s active site (C107XXC110) and Cys78 of ScoI’s copper-binding site (C74XXXC78). We conclude that TlpA recycles ScoI to the dithiol form prior to metallation. Structured summary of protein interactionsTlpAredox reacts with ScoI by oxidoreductase assay (View interaction)ScoI and TlpAbind by cross-linking study (View Interaction: 1, 2)
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