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Enzymatic ω-Oxidation
Open accessAbstract
Abstract The separation of the soluble ω-hydroxylation system of Pseudomonas oleovorans into three components is reported in this paper. They have been identified as rubredoxin (a red protein containing nonheme iron but no inorganic sulfide), a diphosphopyridine nucleotide-rubredoxin reductase, and the ω-hydroxylase. All three proteins are required for the conversion of laurate to ω-hydroxylaurate or of octane to n-octanol in the presence of Fe++ ions, reduced diphosphopyridine nucleotide, and molecular oxygen.
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Cited by
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
Shanklin, J., Achim, C., Schmidt, H., Fox, B. G., & Münck, E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.2981 · Cited by 185
Tsai, Y.-F., Luo, W.-I., Chang, J.-L., Chang, C.-W., Chuang, H.-C., Ramu, R., Wei, G.-T., Zen, J.-M., & Yu, S. S.-F. (2017) · Scientific Reports · doi:10.1038/s41598-017-08610-w · Cited by 31
Hoschek, A., Bühler, B., & Schmid, A. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.27006 · Cited by 26
Peters, J., & Witholt, B. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)00216-9 · Cited by 9
Metadata
- Authors
- Peterson, J. A., Basu, D., & Coon, M. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1966-11
- Volume
- 241
- Issue
- 21
- Pages
- 5162-5164
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1545952675
- Cited by
- 247
- References
- 0
- FWCI
- 15.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
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