Crossref journal-article
Portland Press Ltd.
Biochemical Journal (288)
Abstract

1. The kinetic mechanism of formate dehydrogenase is a sequential pathway. 2. The binding of the substrates proceeds in an obligatory order, NAD+ binding first, followed by formate. 3. It seems most likely that the interconversion of the central ternary complex is extremely rapid, and that the rate-limiting step is the formation or possible isomerization of the enzyme–coenzyme complexes. 4. The secondary plots of the inhibitions with HCO3− and NO3− are non-linear, which suggests that more than one molecule of each species is able to bind to the same enzyme form. 5. The rate of the reverse reaction with carbon dioxide at pH6.0 is 20 times that with bicarbonate at pH8.0, although no product inhibition could be detected with carbon dioxide. The low rate of the reverse reaction precluded any steady-state analysis as the enzyme concentrations needed to obtain a measurable rate are of the same order as the Km values for NAD+ and NADH.

Bibliography

Peacock, D., & Boulter, D. (1970). Kinetic studies of formate dehydrogenase. Biochemical Journal, 120(4), 763–769.

Authors 2
  1. D. Peacock (first)
  2. D. Boulter (additional)
References 0 Referenced 36

None

Dates
Type When
Created 10 years ago (Aug. 10, 2015, 3:30 p.m.)
Deposited 3 years, 9 months ago (Nov. 26, 2021, 9:40 a.m.)
Indexed 3 weeks, 4 days ago (Aug. 5, 2025, 8:51 a.m.)
Issued 54 years, 8 months ago (Dec. 1, 1970)
Published 54 years, 8 months ago (Dec. 1, 1970)
Published Print 54 years, 8 months ago (Dec. 1, 1970)
Funders 0

None

@article{Peacock_1970, title={Kinetic studies of formate dehydrogenase}, volume={120}, ISSN={0306-3283}, url={http://dx.doi.org/10.1042/bj1200763}, DOI={10.1042/bj1200763}, number={4}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Peacock, D. and Boulter, D.}, year={1970}, month=dec, pages={763–769} }