Rat liver “cytochrome b9” is sulfite oxidase.

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Sulfite oxidase activity of cytochrome c: Role of hydrogen peroxide

In humans, sulfite is generated endogenously by the metabolism of sulfur containing amino acids such as methionine and cysteine. Sulfite is also formed from exposure to sulfur dioxide, one of the major environmental pollutants. Sulfite is used as an antioxidant and preservative in dried fruits, vegetables, and beverages such as wine. Sulfite is also used as a stabilizer in many drugs. Sulfite t...

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When isolated mitochondria which have been labeled with [3H]leucine are solubilized and treated with anti-serum specific for cytochrome c oxidase, labeled polypeptides which correspond to the three largest polypeptides of this enzyme are immunoprecipitated. This indicates that the three largest polypeptides of cytochrome c oxidase which have Mr of 66,000, 39,000, and 23,000 are synthesized by i...

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Cytochrome c oxidase is preferentially synthesized in the rough endoplasmic reticulum--mitochondrion complex in rat liver.

The specific activity and content of cytochrome oxidase in the rough endoplasmic reticulum--mitochondrion complex are higher than in the mitochondrial fraction. Radiolabelling studies with the use of hepatocytes and isolated microsomal and rough endoplasmic reticulum--mitochondrion fractions, followed by immunoprecipitation with anti-(cytochrome oxidase) antibody, reveal that the nuclear-coded ...

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Electron paramagnetic resonance of the tungsten derivative of rat liver sulfite oxidase.

Sulfite oxidase purified from livers of tungsten-treated rats has been used for EPR studies of tungsten substituted at the molybdenum site of the enzyme in a fraction of the molecules. The EPR signal of W(V) in sulfite oxidase is quite similar to that of Mo(V) in its line shape and in its sensitivity to the presence of anions such as phosphate and fluoride. Hyperfine interaction with a dissocia...

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Hepatic Sulfite Oxidase

Sulfite oxidase (EC 1.8.3.1), when reduced by sulfite, exhibited the electron paramagnetic resonance spectrum of molybdenum(V). Specific calorimetric analyses demonstrated that the purified enzyme contained 1 molybdenum per heme. The electron paramagnetic resonance signal of molybdenum, which was generated by the addition of sulfite, was enriched by the purification procedure to the same degree...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1981

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)68701-6