The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation
Open accessAbstract
1. A methylene hydroxylase system from camphor induced Pseudomonas putida strain C1 cells has been separated into three fractions: a putidaredoxin reductase, putidaredoxin (an iron-sulfur protein), and a hydroxylase (shown to be a soluble cytochrome P-450). 2. This system of enzymes catalyzes the hydroxylation of methylene carbon 5 of camphor with reduced disphosphopyridine nucleotide as a primary electron donor and molecular oxygen as acceptor. 3. The redoxin serves as the electron carrier from the reduced pyridine nucleotide and reductase to the cytochrome P-450-substrate complex. 4. The coupling of the hydroxylase (P-450) to the reduced diphosphopyridine nucleotide dehydrogenase (reductase), and the putidaredoxin is demonstrated, and substrate is shown to be required for the over-all reaction.
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Cites
The Carbon Monoxide-binding Pigment of Liver Microsomes
Omura, T., & Sato, R. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82244-3 · Cited by 11,781
Estimation of the molecular weights of proteins by Sephadex gel-filtration
Andrews, P. (1964) · Biochemical Journal · doi:10.1042/bj0910222 · Cited by 3,899
Pigments of rat liver microsomes
Klingenberg, M. (1958) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(58)90436-3 · Cited by 664
Lu, A. Y. H., & Coon, M. J. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)56992-7 · Cited by 627
Photochemical Action Spectrum of the Terminal Oxidase of Mixed Function Oxidase Systems
Cooper, D. Y., Levin, S., Narasimhulu, S., Rosenthal, O., & Estabrook, R. W. (1965) · Science · doi:10.1126/science.147.3656.400 · Cited by 501
Peterson, J. A., Basu, D., & Coon, M. J. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99684-5 · Cited by 247
Hedegaard, J., & GUNSALUS, I. C. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97147-4 · Cited by 148
Self-citationAppleby, C. A., & Morton, R. K. (1959) · Biochemical Journal · doi:10.1042/bj0730539 · Cited by 112
Isolation and properties of cytochrome b5 from pig liver
Garfinkel, D. J. (1957) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(57)90012-7 · Cited by 49
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Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Cytochrome P450 systems—biological variations of electron transport chains
Hannemann, F., Bichet, A., Ewen, K. M., & Bernhardt, R. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.07.017 · Cited by 759
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633
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Veith, A., & Moorthy, B. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.10.003 · Cited by 363
Metadata
- Authors
- Katagiri, M., Ganguli, B. N., & Gunsalus, I. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1968-06
- Volume
- 243
- Issue
- 12
- Pages
- 3543-3546
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1603225698
- Cited by
- 437
- References
- 9
- FWCI
- 27.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Katagiri, M., Ganguli, B. N., & Gunsalus, I. C. (1968). A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)93343-0
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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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