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Cited by 94

The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.

Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron

De Jong, L., Albracht, S.P.J., Kemp, A.·1982·Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
DOI 10.1016/0167-4838(82)90162-5
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Abstract

In agreement with others (Myllylä, R., Kuutti-Savolainen, E.-R. and Kivirikko, K.I. (1978) Biochem. Biophys. Res. Commun. 83, 441-448), it was found that, in the absence of ascorbate, prolyl 4-hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) catalyses the hydroxylation of peptidyl proline, stoicheiometrically coupled to the oxidative decarboxylation of 2-oxoglutarate, at a high initial rate. Under these conditions the enzyme becomes inactivated by at least 90% within 1 min in the presence of 400 microM 2-oxoglutarate, in the presence or absence of the peptide substrate (Pro-Pro-Gly)10. The enzyme can be partly reactivated by ascorbate, but not by Fe2+. Addition of a stoicheiometric amount of iron to the enzyme gives rise to a small EPR signal at g = 4.3, which is typical of a high-spin d 5 ion in a rhombic environment. After subsequent incubation for 30 s at 37 degrees C in the presence of 2-oxoglutarate, the amplitude of the EPR signal at g = 4.3 increases 3-4-fold and corresponds to virtually all of the iron added. In addition, an EPR signal at g = 2.0 is formed under these conditions. The signal at g = 4.3 decreases after subsequent addition of ascorbate. It is concluded that in the presence of 2-oxoglutarate enzyme-bound Fe2+ is rapidly converted to Fe3+, leading to inactivation of the enzyme. Enzyme-bound Fe3+ can be reduced again by ascorbate, thus reactivating the enzyme, or, in the absence of 2-oxoglutarate, by…

Overview

Integrity signals

Registry

Crossref · 10.1016/0167-4838(82)90162-5

Cites

15 of 15 references verified0 citation errors · 0 not checkable

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Verification

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Citations

Cites

Research works printed but not linked: 3

  1. Kivirikko, 1980, vol. 1, 53
  2. Counts, 1978, 75, 2145
  3. Bors, 1980, vol. 11B, 1

Cited by

See all 94

Metadata

Authors
De Jong, L., Albracht, S. P. J., & Kemp, A.
Venue
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher
Elsevier BV
Published
1982-06
Volume
704
Issue
2
Pages
326-332
ISSN
0167-4838
DOI
10.1016/0167-4838(82)90162-5
Cited by
94
References
15
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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Data sources

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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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