Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. II. Properties of adenosine-5′-phosphosulfate reductase
1970 ◽
Vol 48
(3)
◽
pp. 344-354
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Keyword(s):
Adenosine-5′-phosphosulfate (APS) reductase was purified from Thiobacillus thioparus extracts 25- to 46-fold and the properties were studied. The molecular weight was 170 000 and the enzyme had 1 mole of FAD, 8–10 moles of iron, and 4–5 moles of labile sulfide. Cytochrome c as well as ferricyanide served as the electron acceptor. The pH optimum shifted from 7.4 to 9.5 when cytochrome c was used instead of ferricyanide. The Km values for sulfite and AMP were reduced from 2.5 mM and 100 μM to 17 μM and 2.5 μM, respectively, with cytochrome c as electron acceptor. Properties of the T. thioparus enzyme were compared to those of APS reductase isolated from Thiobacillus denitrificans and Desulfovibrio desulfuricans.
1971 ◽
Vol 49
(10)
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pp. 1125-1130
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Keyword(s):
1970 ◽
Vol 48
(3)
◽
pp. 334-343
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Keyword(s):
1970 ◽
Vol 48
(3)
◽
pp. 355-363
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1974 ◽
Vol 31
(01)
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pp. 072-085
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1990 ◽
Vol 55
(12)
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pp. 2987-2999
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1974 ◽
Vol 52
(3)
◽
pp. 231-240
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