2012
DOI: 10.1002/cbdv.201200010
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Kinetic and Thermodynamic Effects of Mutations of Human Sulfite Oxidase

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Cited by 15 publications
(12 citation statements)
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“…Unlike other fatal hSO mutations that have been studied (22, 25, 26), the data for purified R309H do not reveal any obvious reasons for this mutation causing sulfite oxidase deficiency. The midpoint potentials of Fe and Mo are somewhat increased, K m sulfite is slightly increased, the activity is increased, and the enzyme still shows IET, although the rates are slow compared to wt.…”
Section: Resultscontrasting
confidence: 64%
See 1 more Smart Citation
“…Unlike other fatal hSO mutations that have been studied (22, 25, 26), the data for purified R309H do not reveal any obvious reasons for this mutation causing sulfite oxidase deficiency. The midpoint potentials of Fe and Mo are somewhat increased, K m sulfite is slightly increased, the activity is increased, and the enzyme still shows IET, although the rates are slow compared to wt.…”
Section: Resultscontrasting
confidence: 64%
“…For example, mutation of H337 and W338 on the surface of the Mo domain influence the potential of the heme domain, despite the large distance between these residues and the heme in the crystal structure (18). Mutations such as K322R, W338A, H337R, and ΔKVATV, show IET rates that are much less than wt hSO and sometimes less their own k cat values, while k cat in many cases has increased significantly as compared to wt (17, 18, 25). These results illustrate the complexity of hSO and indicate that the roles of conformational change and other factors in the catalytic cycle and IET reactions of hSO and their relationship to isolated sulfite oxidase deficiency are yet to be understood.…”
Section: Introductionmentioning
confidence: 99%
“…Mitochondrial SO catalyzes the oxidation of sulfite to sulfate by transferring an atom of oxygen from water to sulfite, and in the process, the enzyme undergoes a two-electron reduction (31). The resultant electrons are then transferred from the enzyme to cytochrome c and on to complex IV, thereby coupling sulfite oxidation (and concentration) to oxygen availability ( Fig.…”
Section: H 2 S Thiosulfate and Oxygen Sensingmentioning
confidence: 99%
“…Sulfite oxidase: SO in the mitochondrial intermembrane space catalyzes the oxidation of sulfite to sulfate by transferring an atom of O 2 from water to sulfite and in the process, the enzyme undergoes a two-electron reduction (140). These electrons are then transferred from SO to cytochrome C and then into the electron transport chain, effectively inversely coupling sulfite concentration to O 2 availability.…”
Section: Effectors Of H 2 S Metabolismmentioning
confidence: 99%