The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Nature of O2 and CO binding to metalloporphyrins and heme proteins.
Open accessAbstract
The O2 vibration of dioxygen adducts of Fe and Co model complexes of alpha,alpha,alpha,alpha-tetrapivalamidophenylporphyrin ("picket fence" porphyrin, TpivPP) with 1-methylimidazole and 1-tritylimidazole as axial bases are reported, obtained with difference techniques between 16O2, 18O2, 169-18O, and NO with a Fourier transform infrared spectrometer. Assignments of upsilono2 are (O2)Fe(TpivPP) 1-methylimidazole, 1159 cm-1 in Nujol; (O2)Fe(TpivPP) 1-tritylimidazole, 1163 in benzene; (O2)Co(TpivPP) 1-methylimidazole, 1150 in Nujol; (O2)Co(TpivPP) 1-tritylimidazole, 1153 in benzene. Comparisons with other known Fe, Co, Cr, and Ti dioxygen complexes are made, and it is concluded that the bent dioxygen ligand is best viewed as bound superoxide, O2-. The CO affinities of various hemoproteins and model systems are discussed. A correlation between the CO stretching frequency and its binding constant is described. The drastically lowered affinity of hemoproteins for CO compared with unencumbered models is attributed to steric hindrance in the distal binding site, which allows discrimination between the already bent FeIII-O2- and the normally linear FeII-CO systems. If the affinity of hemoproteins in living systems for CO relative to O2 were not decreased, then massive poisoning would result from endogenous CO.
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Cites
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Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
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Self-citationFukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389
Varnell, J. A., Tse, E. C. M., Schulz, C. E., Fister, T. T., Haasch, R. T., Timoshenko, J., Frenkel, A. I., & Gewirth, A. A. (2016) · Nature Communications · doi:10.1038/ncomms12582 · Cited by 317
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function
Adam, S. M., Wijeratne, G. B., Rogler, P. J., Diaz, D. E., Quist, D. A., Liu, J. J., & Karlin, K. D. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00074 · Cited by 264
Metadata
- Authors
- Collman, J. P., Brauman, J. I., Halbert, T. R., & Suslick, K. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1976-10
- Volume
- 73
- Issue
- 10
- Pages
- 3333-3337
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2050519643
- Cited by
- 310
- References
- 13
- FWCI
- 16.14
- Type
- journal article
- Language
- en
- Open access
- green
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- Collman, J. P., Brauman, J. I., Halbert, T. R., & Suslick, K. S. (1976). Nature of O2 and CO binding to metalloporphyrins and heme proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.73.10.3333
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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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