By Ryan J. Huxtable
There might be few components with a biochemistry as coherent as that of sulfur. this crucial point is essential to myriad facets of metabo lism, catalysis, and constitution. The plurality of features during which sulfur is concerned derives squarely from the various oxidation states during which it may possibly exist, a few having nice balance, a few being in a position to prepared redox interconversions, and but others having nice instability. for that reason, the flux of sulfur from the geosphere throughout the numerous kingdoms of existence leaves few biochemical procedures unaffected. even if there are huge gaps within the cloth of our easy wisdom of sulfur biochemistry, it really is sufficiently framed to permit a unified and arranged tale, a narrative which a number of the best-known names in bio chemistry have helped to jot down. it's been either a job and a privilege to attempt and summarize this tale, one who is big, complicated, quick relocating, nonetheless constructing and, chiefly, intriguing. i assume that no mo nographer of this kind of massive topic will be chuffed together with his efforts. it's regrettably possible that during making an attempt this job i've got made as many mistakes as a Stilton cheese has blue streaks, and as many omissions as a Swiss cheese has holes. Perfection isn't really to be completed in a monograph. Inasmuch as i've got succeeded, the credits belongs to these whose efforts gave us the information we now have. the place i've got failed, the fault is barely mine.
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Additional resources for Biochemistry of Sulfur
1979). Alternatively, polysulfide or thiosulfate may be formed as intermediates. The formation of thiosulfate involves a flavocytochrome C in Chromatium and Chlorobium. Thiosulfate can disproportionate to sulfite plus elemental sulfur (Schedel and Triiper, 1980). Thiosulfate can be used by Chromatiaceae and Rhodospirillaceae, and, to a lesser extent, by Chlorobiaceae. Thiosulfate can equilibrate with tetrathionate, although few species can oxidize tetrathionate directly. These intermediates may be excreted.
Its MW is approximately 65,000. __ __, Succlnyl CoA Homoser Figure 2-14. Transsulfuration in enteric bacteria. Double bars indicate steps regulated by Met. Table 2-3. 5 mM (Lawrence, 1972). As is appropriate for an enzyme which controls the flow of substrate towards Hey, it is allosterically regulated by both Met and AdoMet. The next enzyme in the pathway is cystathionine y-synthase, catalyzing the reaction given by Equation 2-13: Succinylhomoserine + Cys =:; Cystathionine + Succinate (2-13) This enzyme has been isolated from Salmonella as a pale yellow protein of MW 160,000 with an absorption maximum of 422 nm (Kaplan and Guggenheim, 1971; Kaplan and Flavin, 1966b).
Sulfuydrylase activity is repressed by growth on Met (Robichon-Szulmajster and Surdin-Kerjan, 1971). The enzyme is absent from a Met auxotroph. However, -y-synthase activity is absent from the same auxotroph. The purified enzyme cannot utilize Cys and is not subject to allosteric inhibition (Savin and Flavin, 1972; Laduron, 1972). It thus appears that yeasts have alternative pathways to Hey, Neurospora using a -y-synthase route and Saccharomyces a sulfuydrylase route. 4 Regulation of Methionine Biosynthesis Enteric bacteria and yeasts control Met biosynthesis in different ways.
Biochemistry of Sulfur by Ryan J. Huxtable