INHIBITOR, ISOTOPIC AND KINETIC STUDIES OF HYDROGEN DEHYDROGENASE
Journal Article
·
· Biochimica et Biophysica Acta (Netherlands)
The oxidized form of hydrogen dehydrogenase of Hydrogenomonas ruhlandii was inhibited by BAL, cyanide, dithionite, suifide, sulfite, and thioglycolate. Reduction of the dehydrogenase with DPNH or H/sub 2/ resulted in a diminished effect of the inhibitors, with the exception of p-chloromercuribenzoate, which inhibited only the reduced enzyme. Information from kinetic analysis and inhibitor studies indicated that the enzyme is reduced with H/sub 2/ to give a proton and that this is followed by the oxidation of the reduced enzyme with DPN to give DPNH. The enzyme catalyzes an exchange between H/sub 2/ and HTO and also between HTO and DPNH. Analysis of DPN enzymically reduced T/sub 2/ showed that T is in the BETA -position of DPNH. The enzyme action has a lag phase, which can be eliminated by preincubation with H/sub 2/ or DPNH. (auth)
- Research Organization:
- Yale Univ., New Haven
- NSA Number:
- NSA-17-019793
- OSTI ID:
- 4724593
- Journal Information:
- Biochimica et Biophysica Acta (Netherlands), Journal Name: Biochimica et Biophysica Acta (Netherlands) Vol. Vol: 67; ISSN BBACA
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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