ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

Cytochrome P450 and Aromatic Bases: A 1H NMR Study

Cite this: J. Am. Chem. Soc. 1994, 116, 11, 4866–4873
Publication Date (Print):June 1, 1994
https://doi.org/10.1021/ja00090a035
    ACS Legacy Archive

    Article Views

    193

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Note: In lieu of an abstract, this is the article's first page.

    Free first page

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Cited By

    This article is cited by 30 publications.

    1. Kip P. Conner, Alex A. Cruce, Matthew D. Krzyaniak, Alina M. Schimpf, Daniel J. Frank, Paul Ortiz de Montellano, William M. Atkins, and Michael K. Bowman . Drug Modulation of Water–Heme Interactions in Low-Spin P450 Complexes of CYP2C9d and CYP125A1. Biochemistry 2015, 54 (5) , 1198-1207. https://doi.org/10.1021/bi501402k
    2. Arthur G. Roberts,, M. Dolores Díaz,, Jed N. Lampe,, Laura M. Shireman,, Jeffrey S. Grinstead,, Michael J. Dabrowski,, Josh T. Pearson,, Michael K. Bowman,, William M. Atkins, and, A. Patricia Campbell. NMR Studies of Ligand Binding to P450eryF Provides Insight into the Mechanism of Cooperativity. Biochemistry 2006, 45 (6) , 1673-1684. https://doi.org/10.1021/bi0518895
    3. Gérard Simonneaux and, Arnaud Bondon. Mechanism of Electron Transfer in Heme Proteins and Models:  The NMR Approach. Chemical Reviews 2005, 105 (6) , 2627-2646. https://doi.org/10.1021/cr030731s
    4. Susan Sondej Pochapsky,, Thomas C. Pochapsky, and, Julie W. Wei. A Model for Effector Activity in a Highly Specific Biological Electron Transfer Complex:  The Cytochrome P450cam−Putidaredoxin Couple,. Biochemistry 2003, 42 (19) , 5649-5656. https://doi.org/10.1021/bi034263s
    5. Antonio Donaire,, Jesús Salgado, and, José-María Moratal. Determination of the Magnetic Axes of Cobalt(II) and Nickel(II) Azurins from 1H NMR Data:  Influence of the Metal and Axial Ligands on the Origin of Magnetic Anisotropy in Blue Copper Proteins. Biochemistry 1998, 37 (24) , 8659-8673. https://doi.org/10.1021/bi971974f
    6. K. R. Korzekwa,, N. Krishnamachary,, M. Shou,, A. Ogai,, R. A. Parise,, A. E. Rettie,, F. J. Gonzalez, and, T. S. Tracy. Evaluation of Atypical Cytochrome P450 Kinetics with Two-Substrate Models:  Evidence That Multiple Substrates Can Simultaneously Bind to Cytochrome P450 Active Sites. Biochemistry 1998, 37 (12) , 4137-4147. https://doi.org/10.1021/bi9715627
    7. Sonia Poli-Scaife,, Roger Attias,, Patrick M. Dansette, and, Daniel Mansuy. The Substrate Binding Site of Human Liver Cytochrome P450 2C9:  An NMR Study. Biochemistry 1997, 36 (42) , 12672-12682. https://doi.org/10.1021/bi970527x
    8. Corinne Mouro,, Christiane Jung,, Arnaud Bondon, and, Gérard Simonneaux. Comparative Fourier Transform Infrared Studies of the Secondary Structure and the CO Heme Ligand Environment in Cytochrome P-450cam and Cytochrome P-420cam. Biochemistry 1997, 36 (26) , 8125-8134. https://doi.org/10.1021/bi9700173
    9. S. Modi,, M. J. Paine,, M. J. Sutcliffe,, L.-Y. Lian,, W. U. Primrose,, C. R. Wolf, and, G. C. K. Roberts. A Model for Human Cytochrome P450 2D6 Based on Homology Modeling and NMR Studies of Substrate Binding. Biochemistry 1996, 35 (14) , 4540-4550. https://doi.org/10.1021/bi952742o
    10. Renee M. Chabin,, Ermenegilda McCauley,, Jimmy R. Calaycay,, Theresa M. Kelly,, Karen L. MacNaul,, Gloria C. Wolfe,, Nancy I. Hutchinson,, Sayyaparaju Madhusudanaraju,, John A. Schmidt,, John W. Kozarich, and, Kenny K. Wong. Active-Site Structure Analysis of Recombinant Human Inducible Nitric Oxide Synthase Using Imidazole. Biochemistry 1996, 35 (29) , 9567-9575. https://doi.org/10.1021/bi960476o
    11. Andrew J. Pell, Guido Pintacuda, Clare P. Grey. Paramagnetic NMR in solution and the solid state. Progress in Nuclear Magnetic Resonance Spectroscopy 2019, 111 , 1-271. https://doi.org/10.1016/j.pnmrs.2018.05.001
    12. Ivano Bertini, Claudio Luchinat, Giacomo Parigi, Enrico Ravera. Relaxation. 2017, 77-126. https://doi.org/10.1016/B978-0-444-63436-8.00004-1
    13. Debashree Basudhar, Yarrow Madrona, Sylvie Kandel, Jed N. Lampe, Clinton R. Nishida, Paul R. Ortiz de Montellano. Analysis of Cytochrome P450 CYP119 Ligand-dependent Conformational Dynamics by Two-dimensional NMR and X-ray Crystallography. Journal of Biological Chemistry 2015, 290 (16) , 10000-10017. https://doi.org/10.1074/jbc.M114.627935
    14. Emre M. Isin, F. Peter Guengerich. Substrate binding to cytochromes P450. Analytical and Bioanalytical Chemistry 2008, 392 (6) , 1019-1030. https://doi.org/10.1007/s00216-008-2244-0
    15. Dongmei Cheng, Danni Harris, James R. Reed, Wayne L. Backes. Inhibition of CYP2B4 by 2-ethynylnaphthalene: Evidence for the co-binding of substrate and inhibitor within the active site. Archives of Biochemistry and Biophysics 2007, 468 (2) , 174-182. https://doi.org/10.1016/j.abb.2007.07.032
    16. Shakunthala Narasimhulu. Differential behavior of the sub-sites of cytochrome 450 active site in binding of substrates, and products (implications for coupling/uncoupling). Biochimica et Biophysica Acta (BBA) - General Subjects 2007, 1770 (3) , 360-375. https://doi.org/10.1016/j.bbagen.2006.09.018
    17. William M. Atkins. NON-MICHAELIS-MENTEN KINETICS IN CYTOCHROME P450-CATALYZED REACTIONS. Annual Review of Pharmacology and Toxicology 2005, 45 (1) , 291-310. https://doi.org/10.1146/annurev.pharmtox.45.120403.100004
    18. William M Atkins. Implications of the allosteric kinetics of cytochrome P450s. Drug Discovery Today 2004, 9 (11) , 478-484. https://doi.org/10.1016/S1359-6446(04)03072-7
    19. Moon‐Young Yoon, A. Patricia Campbell, William M. Atkins. “Allosterism” in the Elementary Steps of the Cytochrome P450 Reaction Cycle. Drug Metabolism Reviews 2004, 36 (2) , 219-230. https://doi.org/10.1081/DMR-120033998
    20. Kenneth Korzekwa. In Vitro Enzyme Kinetics Applied to Drug-Metabolizing Enzymes. 2001, 33-54. https://doi.org/10.1201/b14003-3
    21. . Relaxation. 2001, 75-118. https://doi.org/10.1016/S1873-0418(01)80004-X
    22. Magang Shou, Renke Dai, Dan Cui, Kenneth R. Korzekwa, Thomas A. Baillie, Thomas H. Rushmore. A Kinetic Model for the Metabolic Interaction of Two Substrates at the Active Site of Cytochrome P450 3A4. Journal of Biological Chemistry 2001, 276 (3) , 2256-2262. https://doi.org/10.1074/jbc.M008799200
    23. Shiro Yoshioka, Satoshi Takahashi, Koichiro Ishimori, Isao Morishima. Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site. Journal of Inorganic Biochemistry 2000, 81 (3) , 141-151. https://doi.org/10.1016/S0162-0134(00)00097-0
    24. Corinne Mouro, Arnaud Bondon, Christiane Jung, Jacques D. De Certaines, Gérard Simonneaux. Assignment of heme methyl 1 H‐NMR resonances of high‐spin and low‐spin ferric complexes of cytochrome P450cam using one‐dimensional and two‐dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments. European Journal of Biochemistry 2000, 267 (1) , 216-221. https://doi.org/10.1046/j.1432-1327.2000.00995.x
    25. Sovitj Pou, Lori Keaton, Wanida Surichamorn, Gerald M. Rosen. Mechanism of Superoxide Generation by Neuronal Nitric-oxide Synthase. Journal of Biological Chemistry 1999, 274 (14) , 9573-9580. https://doi.org/10.1074/jbc.274.14.9573
    26. Shakunthala Narasimhulu, Lisa M. Havran, Paul H. Axelsen, Jeffery D. Winkler. Interactions of Substrate and Product with Cytochrome P450: P4502B4versus P450cam. Archives of Biochemistry and Biophysics 1998, 353 (2) , 228-238. https://doi.org/10.1006/abbi.1998.0650
    27. . 1 H‐NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate β proton. FEBS Letters 1997, 203-208. https://doi.org/10.1016/S0014-5793(97)00995-2
    28. Iain D.G. Macdonald, W. Ewen Smith, Andrew W. Munro. Inhibitor/fatty acid interactions with cytochrome P‐450 BM3. FEBS Letters 1996, 396 (2-3) , 196-200. https://doi.org/10.1016/0014-5793(96)01095-2
    29. K. Wakasugi, K. Ishimori, I. Morishima. NMR studies of recombinant cytochrome P450cam mutants. Biochimie 1996, 78 (8-9) , 763-770. https://doi.org/10.1016/S0300-9084(97)82534-5
    30. Lucia Banci, Ivano Bertini, Kara L. Bren, Harry B. Gray, Paola Turano. pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein. Chemistry & Biology 1995, 2 (6) , 377-383. https://doi.org/10.1016/1074-5521(95)90218-X

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect