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• W1968667329 endingPage "118" @default.
• W1968667329 startingPage "108" @default.
• W1968667329 abstract "Sulfite dehydrogenase (SDH) from Starkeya novella is a heterodimeric enzyme comprising a Mo active site and a heme c electron relay, which mediates electron transfer from the Mo cofactor to cytochrome c following sulfite oxidation. Studies on the wild type enzyme (SDHWT) and its variants have identified key amino acids at the active site, specifically Arg-55 and His-57. We report the MoVI/V, MoV/IV and FeIII/II (heme) redox potentials of the variants SDHR55K, SDHR55M, SDHR55Q and SDHH57A in comparison with those of SDHWT. For SDHR55M, SDHR55Q and SDHH57A the heme potentials are lowered from ca. 240 mV in SDHWT to ca. 200 mV, while the heme potential in SDHR55K remains unchanged and the Mo redox potentials are not affected significantly in any of these variants. Protein film voltammetry reveals a pH dependence of the electrochemical catalytic half-wave potential (Ecat) of −59 mV/pH in SDHWT and SDHR55K which tracks the pH dependence of the MoVI/V redox potential. By contrast, the catalytic potentials for SDHR55M and SDHH57A are pH-independent and follow the potential of the heme cofactor. These results highlight a switch in the pathway of electron exchange as a function of applied potential that is revealed by protein film voltammetry where an actuation of rate limiting intramolecular electron transfer (IET, Mo to heme) at high potential attenuates the catalytic current relative to faster, direct electron transfer (Mo to electrode) at lower potential. The same change in electron transfer pathway is linked to an unusual peak-shaped profile of the ideally sigmoidal steady state voltammogram in SDHWT alone, which has been associated with a potential dependent change in the orientation of the enzyme on the electrode surface. All other variants show purely sigmoidal voltammetry due to their inherently slower turnover numbers which are always lower than IET rates." @default.
• W1968667329 created "2016-06-24" @default.
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• W1968667329 date "2011-01-01" @default.
• W1968667329 modified "2023-09-27" @default.
• W1968667329 title "Short circuiting a sulfite oxidising enzyme with direct electrochemistry: Active site substitutions and their effect on catalysis and electron transfer" @default.
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• W1968667329 doi "https://doi.org/10.1016/j.bbabio.2010.09.005" @default.
• W1968667329 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20863809" @default.
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