Characterization of the kinetics and electron paramagnetic resonance spectroscopic properties of Acidithiobacillus ferrooxidans sulfide:quinone oxidoreductase (SQR)
作者： Yanfei Zhang , Joel H. Weiner
DOI: 10.1016/J.ABB.2014.09.016
关键词:
摘要: Acidithiobacillus ferrooxidans sulfide:quinone oxidoreductase (SQR) catalyzes the oxidation of sulfide to polysulfide chains or elemental sulfur coupled quinone reduction via a non-covalent FAD cofactor. We investigated role using kinetics and EPR spectroscopy. The properties enzyme were compared with alanine and/or serine variants conserved cysteine residues (Cys128, Cys160, Cys356) structurally close cofactor histidine (His132, His198) implicated in function. When pre-steady state was monitored, Cys128 His132 had similar rates wild-type confirming they do not participate reductive half reaction whereas Cys356 His198 greatly reduced activity. Using steady Na2S-dependent decylubiquinone (DUQ) we measured kcat 6.5s(-1) Km (Na2S) 3.0μM 3.4μM. Variants diminished DUQ activity less affected. A neutral flavin semiquinone observed spectrum SQR Na2S which enhanced Cys160Ala variant suggesting presence Cys356-S(γ)-S-C(4A)-FAD adduct. Potentiometric titrations revealed an Em -139±4mV at pH 7.0.
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