The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
ON THE MECHANISM OF THE ACONITASE AND ISOCITRIC DEHYDROGENASE REACTIONS
Open accessAbstract
The following abbreviations will be used: DPN, diphosphopyridine nucleotide; TPN, triphosphopyridine nucleotide; DPNH and TPNH, the reduced forms; DPND and TPND, reduced deuterio-DPN and reduced deuterio-TPN.2 In the experiments of San Pietro et al. (1) the added DPN was only partially reduced by the isocitric dehydrogenase-transhydrogenase system.Labeling apparently resulted from incorporation of deuterium into the remaining DPN during the boiling period after the enzyme reaction had been stopped.This interpretation is based on the following observations made during the course of the present work.1047
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“The enzyme has an asymmetric binding site for citrate, allowing the substrate to bind only in a specific orientation, so the transfer of the OH occurs only if the appropriate orientation conditions are met [112].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [112]
Citations
Cites
Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids
Racker, E. (1950) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(50)90026-6 · Cited by 814
CRYSTALLINE ALCOHOL DEHYDROGENASE FROM BAKERS' YEAST
Racker, E. (1950) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51151-6 · Cited by 622
MICROESTIMATION OF CITRIC ACID; A NEW COLORIMETRIC REACTION FOR PENTABROMOACETONE
Natelson, S., Pincus, J. B., & Lugovoy, J. K. (1948) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57193-3 · Cited by 259
THE ENZYMATIC TRANSFER OF HYDROGEN
Fisher, H. F., Conn, E. E., Vennesland, B., & Westheimer, F. H. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66181-2 · Cited by 240
NEUROSPORA DIPHOSPHOPYRIDINE NUCLEOTIDASE
Kaplan, N. O., Colowick, S. P., & Nason, A. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55952-4 · Cited by 194
Self-citation[116] Isocitric dehydrogenase system (TPN) from pig heart
Ochoa, S. (1955) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(55)01121-x · Cited by 163
THE ENZYMATIC TRANSFER OF HYDROGEN FROM ALCOHOL TO DPN
Westheimer, F. H., Fisher, H. F., Conn, E. E., & Vennesland, B. (1951) · Journal of the American Chemical Society · doi:10.1021/ja01149a561 · Cited by 152
ON THE STRUCTURE OF REDUCED DIPHOSPHOPYRIDINE NUCLEOTIDE
Pullman, M. E., Pietro, A. S., & Colowick, S. P. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71303-3 · Cited by 129
Self-citationMicro-determination of isocitric and cis-aconitic acids in biological material
Krebs, H. A., & Eggleston, L. V. (1944) · Biochemical Journal · doi:10.1042/bj0380426 · Cited by 111
The activation of aconitase by ferrous ions and reducing agents
Morrison, J. F. (1954) · Biochemical Journal · doi:10.1042/bj0580685 · Cited by 107
Research works printed but not linked: 2
- Stern, J. R., in Colowick, S. P., and Kaplan, N. O., Methods in enzymology, New York, 3, 425 (1956).
- Breusch, 1944, Enzymologia, 11, 243
Cited by
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342
Chirality Due to the Presence of Hydrogen Isotopes at Noncyclic Positions
Arigoni, D., & Eliel, E. L. (1969) · Topics in stereochemistry · doi:10.1002/9780470147139.ch4 · Cited by 114
THE ABSOLUTE STEREOCHEMICAL COURSE OF CITRIC ACID BIOSYNTHESIS
Hanson, K. R., & Rose, I. A. (1963) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.50.5.981 · Cited by 103
The Enzymatic Transfer of Hydrogen
Nakamoto, T., & Vennesland, B. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69610-3 · Cited by 87
Purification and Kinetic Studies of Beef Liver Cytoplasmic Aconitase
Henson, C. P., & Cleland, W. W. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95824-2 · Cited by 85
Metadata
- Authors
- Englard, S., & Colowick, S. P.
- Affiliations
- Albert Einstein College of Medicine (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1957-06
- Volume
- 226
- Issue
- 2
- Pages
- 1047-1058
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1544948283
- Cited by
- 47
- References
- 27
- Citations by year
- 2023: 1 · 2015: 1
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- aconitase, isocitrate dehydrogenase, reaction mechanism, deuterium labeling, diphosphopyridine nucleotide, triphosphopyridine nucleotide, enzyme kinetics
- MeSH terms
- Aconitate Hydratase, Hydro-Lyases, Isocitrate Dehydrogenase, Oxidoreductases
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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