The DOI matches its Crossref record.
Antibody-Catalyzed Porphyrin Metallation
Abstract
An antibody elicited to a distorted N -methyl porphyrin catalyzed metal ion chelation by the planar porphyrin. At fixed Zn 2+ and Cu 2+ concentrations, the antibody-catalyzed reaction showed saturation kinetics with respect to the substrate mesoporphyrin IX (2) and was inhibited by the hapten, N -methylmesoporphyrin IX (1). The turnover number of 80 hour -1 for antibody-catalyzed metallation of 2 with Zn 2+ compares with an estimated value of 800 hour -1 for ferrochelatase. The antibody also catalyzed the insertion of Co 2+ and Mn 2+ into 2, but it did not catalyze the metallation of protoporphyrin IX (3) or deuteroporphyrin IX (4). The antibody has high affinity for several metalloporphyrins, suggesting an approach to developing antibody-heme catalysts for redox or electron transfer reactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
At the Crossroads of Chemistry and Immunology: Catalytic Antibodies
Lerner, R. A., Benkovic, S. J., & Schultz, P. G. (1991) · Science · doi:10.1126/science.2024118 · Cited by 668
Self-citationBinding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes
Houk, K. N., Leach, A. G., Kim, S. P., & Zhang, X. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200200565 · Cited by 586
Engineering Novel Metalloproteins: Design of Metal-Binding Sites into Native Protein Scaffolds
Lu, Y., Berry, S. M., & Pfister, T. D. (2001) · Chemical Reviews · doi:10.1021/cr0000574 · Cited by 375
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
(2001) · Nature Structural Biology · doi:10.1038/84152 · Cited by 227
Metadata
- Authors
- Cochran, A. G., & Schultz, P. G.
- Venue
- Science
- Published
- 1990-08-17
- Volume
- 249
- Issue
- 4970
- Pages
- 781-783
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1973626200
- Cited by
- 189
- References
- 0
- FWCI
- 6.69
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Antibody-Catalyzed Porphyrin Metallation. https://app.cochat.ai/papers/10.1126/science.2389144
- The paper
- Cochran, A. G., & Schultz, P. G. (1990). Antibody-Catalyzed Porphyrin Metallation. Science. https://doi.org/10.1126/science.2389144
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.
