Mechanism of oxidation of tetrahydropterins
Abstract
The oxidation of tetrahydropterins and 7,8-dihydropterins by ferric iron has been examined by both polarographic and spectral techniques. Quinonoid dihydropterin, an intermediate in the oxidation of the tetrahydropterins, is formed rapidly, as is ferrous iron. The quinonoid dihydropterin then rearranges to 7,8-dihydropterin. The rate of oxidation of 7,8-dihydropterins is much slower than that of tetrahydropterins. The reduction potential of the reversible quinonoid dihydropterin – tetrahydropterin couple has been measured and shown to be consistent with the known chemistry of these compounds. Kinetic measurements and structural studies have been used to formulate a mechanism for the oxidation of tetrahydropterins to quinonoid dihydropterins. This mechanism involves abstraction of an electron from position 5, followed by rapid loss of two protons and the other electron.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
BH4 alone, in a co-factor independent manner, can reduce cytochrome-C-Fe3+ to cytochrome-C-Fe2+ at physiological concentrations and efficacy.
“Moreover, we confirmed data from almost 50 years ago that BH4 alone, in a co-factor independent manner, can reduce cytochrome-C-Fe3+ to cytochrome-C-Fe2+ at physiological concentrations and efficacy (Archer et al., 1972; Figure 4).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Archer et al., 1972
Cited by
Sorted by citations
Pterin-Dependent Amino Acid Hydroxylases
Kappock, T. J., & Caradonna, J. P. (1996) · Chemical Reviews · doi:10.1021/cr9402034 · Cited by 325 · see citing works
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
The metabolite BH4 controls T cell proliferation in autoimmunity and cancer
Cronin, S. J. F., Seehus, C., Weidinger, A., Talbot, S., Reissig, S., Seifert, M., Pierson, Y., McNeill, E., Longhi, M. S., Turnes, B. L., et al. (2018) · Nature · doi:10.1038/s41586-018-0701-2 · Cited by 285 · see citing works
N EW P ERSPECTIVES ON F OLATE C ATABOLISM
Suh, J. R., Herbig, A. K., & Stover, P. J. (2001) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.21.1.255 · Cited by 261 · see citing works
Tetrahydrobiopterin Radical Enzymology
Wei, C.-C., Crane, B. R., & Stuehr, D. J. (2003) · Chemical Reviews · doi:10.1021/cr0204350 · Cited by 175 · see citing works
Giovanelli, J., Campos, K. L., & Kaufman, S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7091 · Cited by 162 · see citing works
Structural characterization of a molybdopterin precursor
Wuebbens, M. M., & Rajagopalan, K. V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38676-4 · Cited by 118 · see citing works
Vásquez-Vivar, J., Whitsett, J., Martásek, P., Hogg, N., & Kalyanaraman, B. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00680-3 · Cited by 112 · see citing works
Purification and Properties of a Folate-catabolizing Enzyme
Suh, J. R., Oppenheim, E. W., Girgis, S., & Stover, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005864200 · Cited by 79 · see citing works
Dihydrofolate Reductase: Binding of Substrates and Inhibitors and Catalytic Mechanism
Gready, J. E. (1980) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60007-1 · Cited by 50 · see citing works
Campos, K. L., Giovanelli, J., & Kaufman, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1721 · Cited by 49 · see citing works
Dihydropteridine reductase (DHPR), its cofactors, and its mode of action
Armarego, W. L. F., Randles, D., & Waring, P. (1984) · Medicinal Research Reviews · doi:10.1002/med.2610040302 · Cited by 45 · see citing works
The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase.
Gardlik, S., & Rajagopalan, K. V. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38265-1 · Cited by 39 · see citing works
Batinic̈‐Haberle, I., Spasojević, I., & Fridovich, I. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.041 · Cited by 38 · see citing works
Du, M., Yeh, H.-C., Berka, V., Wang, L.-H., & Tsai, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209606200 · Cited by 37 · see citing works
Gardlik, S., & Rajagopalan, K. V. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67732-x · Cited by 36 · see citing works
Formation of Oxygen Radicals in Solutions of 7,8-Dihydroneopterin
Oettl, K., Wirleitner, B., Baier-Bitterlich, G., Grammer, T. B., Fuchs, D., & Reibnegger, G. J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1520 · Cited by 34 · see citing works
Molybdopterin Radical in Bacterial Aldehyde Dehydrogenases
Luykx, D. M. A. M., Duine, J. A., & de Vries, S. (1998) · Biochemistry · doi:10.1021/bi972972y · Cited by 28 · see citing works
Greatbanks, S. P., Hillier, I. H., Garner, C. D., & JOULE, J. A. (1997) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/a700330g · Cited by 26 · see citing works
Hagedoorn, P., Schmidt, P. P., Andersson, K. K., Hagen, W. R., Flatmark, T., & Martı́nez, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009458200 · Cited by 25 · see citing works
Doyle, W. A., Burke, J. F., Chovnick, A., Dutton, F. L., Whittle, J. R. S., & Bray, R. C. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0782u.x · Cited by 25 · see citing works
Isolation and characterization of quinonoid dihydropterins by high-performance liquid chromatography
Haavik, J., & Flatmark, T. (1983) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)88192-9 · Cited by 19 · see citing works
Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study
Capeillère‐Blandin, C., Mathieu, D., & Mansuy, D. (2005) · Biochemical Journal · doi:10.1042/bj20050437 · Cited by 17 · see citing works
Moore, J., Wood, J. M., & Schallreuter, K. U. (2002) · Journal of Raman Spectroscopy · doi:10.1002/jrs.887 · Cited by 16 · see citing works
Reactions of CO 2 ˙ – radicals with pterin and pterin-6-carboxylate ions
Farahani, M., Surdhar, P. S., Allen, S., Armstrong, D. A., Schöneich, C., Mao, Y., & Asmus, K. (1991) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29910001687 · Cited by 14 · see citing works
474—Electrochemistry of 6,7-dimethylpterins
Ege-Serpkenci, D., & Dryhurst, G. (1982) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(82)80174-8 · Cited by 14 · see citing works
Kall, M. A., Nørgaard, P., Pedersen, S. J., & Leth, T. (2000) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/s0731-7085(00)00327-7 · Cited by 13 · see citing works
New pteridine substrates for dihydropteridine reductase and horseradish peroxidase
Armarego, W. L. F., Ohnishi, A., & Taguchi, H. (1986) · Biochemical Journal · doi:10.1042/bj2340335 · Cited by 12 · see citing works
Study of the tautomerization of quinonoid dihydropterins by liquid chromatography/electrochemistry
Lunte, C. E., & Kissinger, P. T. (1984) · Analytica Chimica Acta · doi:10.1016/s0003-2670(00)84811-4 · Cited by 10 · see citing works
Matsuura, S., Murata, S., & Sugimoto, T. (1986) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)84047-2 · Cited by 10 · see citing works
Pteridine, LX. Synthese und Oxidationsverhalten von 7,8‐Dihydroxanthopterinen
Pfleiderer, W. (1974) · Chemische Berichte · doi:10.1002/cber.19741070305 · Cited by 10 · see citing works
Funahashi, Y., Kato, C., & Yamauchi, O. (1999) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.72.415 · Cited by 9 · see citing works
Lunte, C. E., & Kissinger, P. T. (1984) · Analytical Chemistry · doi:10.1021/ac00268a016 · Cited by 9 · see citing works
Synthesis, Redox and Spectroscopic Properties of Pterin of Molybdenum Cofactors
Colston, K. J., & Basu, P. (2022) · Molecules · doi:10.3390/molecules27103324 · Cited by 7 · see citing works
“Reduced pterins are readily oxidized by strong oxidizing agents to yield fully oxidized pterin if desired [34,35].”
BackgroundBoulghobra, A., & Bonose, M. (2022) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408347.2022.2151833 · Cited by 6 · see citing works
Boulghobra, A., Bonose, M., Alhajji, E., Pallandre, A., Roze, E. F., Baudin, B., Menet, M., & Moussa, F. (2023) · Molecules · doi:10.3390/molecules28031267 · Cited by 5 · see citing works
“These results disagree with a previous hypothesis suggesting that qH2Bip’s isomerization into H2Bip is slower than the loss of the lateral chain leading to H2Ptr, and that is why the isomerization only occurs when qH2Bip is stable enough not to be oxidized into H2Ptr [22].”
BackgroundResultInfluentialGeneration of carbon monoxide and iron from hemeproteins in the presence of 7,8-dihydroneopterin
Horejsi, R., Jung, C., Möller, R., Tafeit, E., & Reibnegger, G. J. (2002) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00206-4 · Cited by 5 · see citing works
“The stability of 7,8-dihydropterins on air is somewhat higher, but their half-life remains also shorter than 1 h [12].”
BackgroundBiosynthesis and Function of Unconjugated Pterins in Mammalian Tissues
Gal, E. M. (1982) · Springer eBooks · doi:10.1007/978-1-4684-7541-8_2 · Cited by 5 · see citing works
Samanta, S., & Mondal, P. (2024) · ChemPhysChem · doi:10.1002/cphc.202400401 · Cited by 1 · see citing works
Horejsi, R., Möller, R., Tafeit, E., & Reibnegger, G. J. (2002) · Pteridines · doi:10.1515/pteridines.2002.13.4.115 · Cited by 1 · see citing works
(1988) · The chemistry of heterocyclic compounds/The Chemistry of heterocyclic compounds · doi:10.1002/9780470186893.refs
Ichinose, M., & Yamada, M. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734378603.793555631
Chandel, N. S. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734378603.793554283
Hunt for NDSRIs: Unveiling Hidden Threats with the Novel 15 N-Enriched NAP Test
Simonetto, A., Monzani, E., Razzetti, G., & Mantegazza, S. (2025) · Organic Process Research & Development · doi:10.1021/acs.oprd.5c00223
Chemical and biological dynamics of natural pterins
Doi, Y. (2026) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbag094
- Authors
- Archer, M. C., Vonderschmitt, D. J., & Scrimgeour, K. G.
- Venue
- Canadian Journal of Biochemistry
- Publisher
- Canadian Science Publishing
- Published
- 1972-11-01
- Volume
- 50
- Issue
- 11
- Pages
- 1174-1182
- ISSN
- 0008-4018 (ISSN-L)
- OpenAlex
- W2114952164
- Cited by
- 45
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2019: 2 · 2018: 2
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Canadian Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- tetrahydropterins, ferrous iron, oxidation mechanism, redox potential, electron abstraction, proton loss, pterin metabolism
- MeSH terms
- Chemistry, Hydrogen-Ion Concentration, Iron, Kinetics, Oxidation-Reduction, Polarography, Pterins, Quinones, Spectrophotometry, Ultraviolet, Chemical Phenomena
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review