Discerning different and opposite effects of hydrogenase on the corrosion of mild steel in the presence of phosphate species

Mild steel coupons were exposed to hydrogenase in a 10mM phosphate solution. Control coupons were covered by a layer of vivianite. The injection of hydrogenase caused a fast increase in the open circuit potential; this increase depended on the amount of hydrogenase injected and increased from 8mV fo...

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Veröffentlicht in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2016-10, Vol.111, p.31-40
Hauptverfasser: Mehanna, Maha, Rouvre, Ingrid, Delia, Marie-Line, Feron, Damien, Bergel, Alain, Basseguy, Régine
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Sprache:eng
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Zusammenfassung:Mild steel coupons were exposed to hydrogenase in a 10mM phosphate solution. Control coupons were covered by a layer of vivianite. The injection of hydrogenase caused a fast increase in the open circuit potential; this increase depended on the amount of hydrogenase injected and increased from 8mV for 30μL hydrogenase to 63mV for 80μL. The presence of enzyme resulted in a thicker deposit: high amounts induced the accumulation of corrosion products. Hydrogenase that was deactivated by air revealed a protective effect: non-degradation was observed. In contrast, hydrogenase that was denatured by heat provoked an important deposit of corrosion products with a heterogeneous, cracked structure. The study showed that the action of hydrogenase is not linked to its regular enzymatic activity but to a balance between the protective effect of its protein shell and the electrochemical action of its iron-sulphur clusters. Depending on the operating conditions, hydrogenase can either enhance or mitigate the formation of a corrosion layer on mild steel. •Hydrogenase increases the corrosion process of mild steel in phosphate medium.•Hydrogenase that was deactivated by air revealed a protective effect.•In contrast, hydrogenase denatured by heating led to a thick deposit with deep cracks.•The iron-sulphur clusters of hydrogenase were suspected to exacerbate corrosion.
ISSN:1567-5394
1878-562X
DOI:10.1016/j.bioelechem.2016.04.005