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Kinetics of cytochrome P-450 reduction: evidence for faster reduction of the high-spin ferric state

Cite this: Biochemistry 1985, 24, 19, 5130–5136
Publication Date (Print):September 1, 1985
https://doi.org/10.1021/bi00340a026
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    Cited By

    This article is cited by 40 publications.

    1. Donovan C. Haines, Amita Hegde, Baozhi Chen, Weiqiang Zhao, Muralidhar Bondlela, John M. Humphreys, David A. Mullin, Diana R. Tomchick, Mischa Machius, and Julian A. Peterson . A Single Active-Site Mutation of P450BM-3 Dramatically Enhances Substrate Binding and Rate of Product Formation. Biochemistry 2011, 50 (39) , 8333-8341. https://doi.org/10.1021/bi201099j
    2. Abhishek Dey, Yonging Jiang, Paul Ortiz de Montellano, Keith O. Hodgson, Britt Hedman and Edward I. Solomon . S K-edge XAS and DFT Calculations on Cytochrome P450: Covalent and Ionic Contributions to the Cysteine-Fe Bond and Their Contribution to Reactivity. Journal of the American Chemical Society 2009, 131 (22) , 7869-7878. https://doi.org/10.1021/ja901868q
    3. Sibylle Brenner,, Sam Hay,, Hazel M. Girvan,, Andrew W. Munro, and, Nigel S. Scrutton. Conformational Dynamics of the Cytochrome P450 BM3/N-Palmitoylglycine Complex:  The Proposed “Proximal−Distal” Transition Probed by Temperature-Jump Spectroscopy. The Journal of Physical Chemistry B 2007, 111 (27) , 7879-7886. https://doi.org/10.1021/jp073036n
    4. F. Peter Guengerich, Clayton J. Wilkey, Thanh T.N. Phan. Human cytochrome P450 enzymes bind drugs and other substrates mainly through conformational-selection modes. Journal of Biological Chemistry 2019, 294 (28) , 10928-10941. https://doi.org/10.1074/jbc.RA119.009305
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    15. Harshica Fernando, James R. Halpert, Dmitri R. Davydov. Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein. Archives of Biochemistry and Biophysics 2008, 471 (1) , 20-31. https://doi.org/10.1016/j.abb.2007.11.020
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