The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
[17] Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
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Citations
Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
Transduction of linked genetic characters of the host by bacteriophage P1
Lennox, E. S. (1955) · Virology · doi:10.1016/0042-6822(55)90016-7 · Cited by 2,584
Porphyrins and Metalloporphyrins
(1978) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80351-3 · Cited by 1,716
Porphyrins and Metalloporphyrins
CRELIN, E. S. (1964) · The Yale Journal of Biology and Medicine · Cited by 992
Molecular Mechanisms of Oxygen Activation
GEARY, P. J. (1975) · Biochemical Society Transactions · doi:10.1042/bst0030218a · Cited by 570
A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation
Katagiri, M., Ganguli, B. N., & Gunsalus, I. C. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93343-0 · Cited by 437
Self-citationCamphor binding by Pseudomonas putida cytochrome P-450
Peterson, J. A. (1971) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(71)90375-4 · Cited by 260
A Simple Serum Iron Method Using the New Sensitive Chromogen Tripyridyl-s-triazine
Fischer, D. S., & Price, D. C. (1964) · Clinical Chemistry · doi:10.1093/clinchem/10.1.21 · Cited by 232
Enzyme activity as an indicator of red cell age
Sass, M. D., Vorsanger, E., & Spear, P. W. (1964) · Clinica Chimica Acta · doi:10.1016/0009-8981(64)90210-4 · Cited by 209
Yu, C.-A., Gunsalus, I. C., Katagiri, M., Suhara, K., & Takemori, S. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43095-0 · Cited by 161
Self-citation
Cited by
Kominami, S., Ochi, H., Kobayashi, Y., & Takemori, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85711-3 · Cited by 171
Reductive dehalogenation by cytochrome P450CAM: Substrate binding and catalysis
Li, S., & Wackett, L. P. (1993) · Biochemistry · doi:10.1021/bi00087a014 · Cited by 80
Heme: the most versatile redox centre in biology?
Chapman, S. K., Daff, S., & Munro, A. W. (1997) · Metal Sites in Proteins and Models · doi:10.1007/3-540-62870-3_2 · Cited by 72
The effect of cytochrome P-450cam on the NMR relaxation rate of water protons.
Philson, S. B., Debrunner, P. G., Schmidt, P. G., & Gunsalus, I. C. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86689-9 · Cited by 49
Self-citationBlocki, F. A., Logan, M. S., Baoli, C., & Wackett, L. P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37043-6 · Cited by 44
Metadata
- Authors
- Gunsalus, I. C., & Wagner, G. C.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1978
- Volume
- 52
- Pages
- 166-188
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W1492818403
- Cited by
- 318
- References
- 16
- FWCI
- 25.42
- Type
- book chapter
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: [17] Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase. https://app.cochat.ai/papers/10.1016/s0076-6879(78)52019-3
- The paper
- Gunsalus, I. C., & Wagner, G. C. (1978). [17] Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods in Enzymology. https://doi.org/10.1016/s0076-6879(78)52019-3
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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.
