The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's
Abstract
Cytochrome P450BM-3, a bacterial fatty acid monooxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an α and a β domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the β domain and the B′ and F helices of the α domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.
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The three‐dimensional structure of retinol‐binding protein.
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Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala
Raag, R., Martinis, S. A., Sligar, S. G., & Poulos, T. L. (1991) · Biochemistry · doi:10.1021/bi00112a008 · Cited by 208
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SIMPSON, E. R., MAHENDROO, M. S., MEANS, G. D., KILGORE, M. W., HINSHELWOOD, M. M., GRAHAM-LORENCE, S., AMARNEH, B., ITO, Y., FISHER, C. R., MICHAEL, M. D., et al. (1994) · Endocrine Reviews · doi:10.1210/edrv-15-3-342 · Cited by 1,537
Congenital adrenal hyperplasia due to 21-hydroxylase deficiency*
White, P. C., & Speiser, P. W. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.3.0398 · Cited by 1,432
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Stuehr, D. J. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00016-x · Cited by 996
Simpson, E. R., Clyne, C., Rubin, G., Boon, W. C., Robertson, K., Britt, K., Speed, C., & Jones, M. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.081601.142703 · Cited by 773
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
Metadata
- Authors
- Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A., & Deisenhofer, J.
- Venue
- Science
- Published
- 1993-08-06
- Volume
- 261
- Issue
- 5122
- Pages
- 731-736
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2000051743
- Cited by
- 877
- References
- 3
- FWCI
- 47.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A., & Deisenhofer, J. (1993). Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's. Science. https://doi.org/10.1126/science.8342039
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