Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase-Reference-Cited by-同舟云学术

Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase

Published:2024-03 Issue:3 Volume:300 Page:105688
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Tateishi Yasuhiro^ORCID,Webb Stephany N.,Li Bian,Liu Lu^ORCID,Lindsey Rose Kristie,Leser Micheal^ORCID,Patel Purvi,Guengerich F. Peter^ORCID

Funder

Vanderbilt University Medical Center

Vanderbilt Institute of Chemical Biology, School of Medicine, Vanderbilt University

National Institutes of Health

Vanderbilt-Ingram Cancer Center

Publisher

Elsevier BV

Reference76 articles.

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3. Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5;Yamazaki;J. Biol. Chem.,1996

4. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer;Auchus;J. Biol. Chem.,1998

5. Stimulation of cytochrome P450 reactions by apo-cytochrome b5: evidence against transfer of heme from cytochrome P450 3A4 to apo-cytochrome b5 or heme oxygenase;Yamazaki;J. Biol. Chem.,2001

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