Biochemistry. by Dunitz J.D. PDF

By Dunitz J.D.

ISBN-10: 0387070532

ISBN-13: 9780387070537

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Maximum stimulation of ATP reduction is observed at approximately 75 o, while no stimulation can be detected at 37 °. The molecular weight determined by gel filtration was approximately 80,000 but no information about the subunit structure is yet available. d. Ribonucleoside Triphosphate Reductase ]rom Pithomyces chartarum The reductase detected in crude extracts of this fungus showed barely detectable activity with pufine nucleoside diphosphates and was most active with ATP and GTP (71). B. Ribonucleoside Diphosphate Reductases Adenosylcobalamin-dependent reductases which utilize ribonucleoside diphosphates as substrates have been detected in three different microorganisms : Rhizobium meliloti (82), Bacillus megaterium (10) and Corynebacterium nephridii (83).

Coli, both enzymes contain 5 half-cystine residues and have almost identicat absorption spectra. Like the E. coli enzyme, thioredoxin reductase from yeast is completely inhibited by p-chloromercuriphenylsulfonate (PCMS) only in the presence of NADPH suggesting that the yeast enzyme also contains a disulfide bridge at the catalytic site. Thioredoxin reductase from calf liver was found to reduce 5,5'dithiobis-(2-nitrobenzoic acid) (DTNB) at the expense of NADPH even in the absence of thioredoxin as an intermediate electron carrier, indicating that this mammalian reductase may have a wider substrate specificity than the corresponding enzymes from E.

These results clearly demonstrate that the enzymatic activity of protein B2 depends on the presence of the organic radical and that the radical in turn depends on the presence of iron (67). Aged preparations of protein B2, which show decreased enzyme activity, with simultaneous loss in radical concentration, but without changes in iron concentration, can be reactivated by removal of the metal followed by reconstitution with ferrous ions. The MSssbauer spectrum of [57Fe] protein B2 as well as the electronic spectrum of protein B2 after treatment with hydroxylamine are very similar to those of methydroxohemerythrin and oxyhemerythrin, suggesting that protein B2 contains two non-identical 27 H.

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Biochemistry. by Dunitz J.D.


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