Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00446a035
Reference37 articles.
1. The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis.
2. Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.
3. Direct evidence for electron transfer from ferrous cytochrome b5 to the oxyferrous intermediate of liver microsomal cytochrome P-450 LM2.
4. Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin.
5. Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase.
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