The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Stereochemistry of Hemes and Other Metalloporphyrins: The remarkably varied stereochemistry of the iron porphyrins is utilized in the hemoprotein function.
Abstract
Metalloporphyrins, most notably the iron porphyrins, observe clearly defined, internally consistent, structural principles that promise to be fully applicable to the hemes in the several families of the hemoproteins.
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Citations
Cites
PERUTZ, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,926
Structural chemistry and molecular biology
Rich, A., Davidson, N., & Pauling, L. C. (1968) · Medical Entomology and Zoology · Cited by 1,702
Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look
Wyman, J. (1964) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60190-4 · Cited by 1,608
PERUTZ, M. F., ROSSMANN, M. G., CULLIS, A. F., MUIRHEAD, H., WILL, G., & NORTH, A. C. T. (1960) · Nature · doi:10.1038/185416a0 · Cited by 1,350
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
WEISS, J. J. (1964) · Nature · doi:10.1038/202083b0 · Cited by 416
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
PAULING, L. (1964) · Nature · doi:10.1038/203182b0 · Cited by 374
MUIRHEAD, H., & PERUTZ, M. F. (1963) · Nature · doi:10.1038/199633a0 · Cited by 330
Crystal and Molecular Structures of Some Metal Tetraphenylporphines
Fleischer, E. B., Miller, C. K., & Webb, L. E. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01066a009 · Cited by 293
An X-ray study of azide methaemoglobin
Perutz, M. F., & Mathews, F. S. (1966) · Journal of Molecular Biology · doi:10.1016/0022-2836(66)90088-x · Cited by 292
Kendrew, J. C. (1963) · Science · doi:10.1126/science.139.3561.1259 · Cited by 291
Cited by
Extended x-ray absorption fine structure—its strengths and limitations as a structural tool
Lee, P. A., Citrin, P. H., Eisenberger, P., & Kincaid, B. M. (1981) · Reviews of Modern Physics · doi:10.1103/revmodphys.53.769 · Cited by 1,878
Vitamin B12: Experiments Concerning the Origin of Its Molecular Structure
Eschenmoser, A. (1988) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198800051 · Cited by 374
The crystal structure of cytochrome c peroxidase.
Poulos, T. L., Freer, S. T., Alden, R. A., Edwards, S. L., Skogland, U., Takio, K., Eriksson, B., Xuong, N., Yonetani, T., & Kraut, J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86214-2 · Cited by 338
Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution
Steigemann, W., & Weber, E. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90332-2 · Cited by 302
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
- Hoard, J. L.
- Venue
- Science
- Published
- 1971-12-24
- Volume
- 174
- Issue
- 4016
- Pages
- 1295-1302
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2029125787
- Cited by
- 302
- References
- 21
- FWCI
- 21.58
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Stereochemistry of Hemes and Other Metalloporphyrins: The remarkably varied stereochemistry of the iron porphyrins is utilized in the hemoprotein function. https://app.cochat.ai/papers/10.1126/science.174.4016.1295
- The paper
- Hoard, J. L. (1971). Stereochemistry of Hemes and Other Metalloporphyrins: The remarkably varied stereochemistry of the iron porphyrins is utilized in the hemoprotein function. Science. https://doi.org/10.1126/science.174.4016.1295
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
