Theoretical insights into the reductive metabolism of CCl4 by cytochrome P450 enzymes and the CCl4-dependent suicidal inactivation of P450

2014 ◽  
Vol 43 (39) ◽  
pp. 14833-14840 ◽  
Author(s):  
Xiao-Xi Li ◽  
Qing-Chuan Zheng ◽  
Yong Wang ◽  
Hong-Xing Zhang
Keyword(s):  
Cytochrome P450 ◽  
Reduction Product ◽  
Cytochrome P450 Enzymes ◽  
Electron Reduction ◽  
The One ◽  
Reductive Metabolism

The one-electron reduction product, ˙CCl3, irreversibly inactivates P450 via covalently binding to the meso-carbon, whereas the two successive one-electron reductions product, :CCl2, reversibly inhibits P450 by coordinating to iron.

Identification of two reduction products of glyoxal bis(2-mercaptoanil)nickel. Characterization of the one-electron reduction product and the partially hydrogenated anion

1967 ◽  
Vol 89 (10) ◽  
pp. 2278-2281 ◽  
Author(s):  
F. Lalor ◽  
M. Frederick. Hawthorne ◽  
August H. Maki ◽  
K. Darlington ◽  
Alan. Davison ◽  
...  
Keyword(s):  
Reduction Product ◽  
Electron Reduction ◽  
The One

scholarly journals EPR and DFT studies of the one-electron reduction product of phospholium cations

2006 ◽  
Vol 8 (7) ◽  
pp. 862-868 ◽  
Author(s):  
Prashant Adkine ◽  
Thibault Cantat ◽  
Eliane Deschamps ◽  
Louis Ricard ◽  
Nicolas Mézailles ◽  
...  
Keyword(s):  
Reduction Product ◽  
Dft Studies ◽  
Electron Reduction ◽  
The One

Cytochrome P450 enzymes: ubiquitous "receptors" for drugs

1991 ◽  
Vol 69 (8) ◽  
pp. 1129-1132 ◽  
Author(s):  
Frank S. LaBella
Keyword(s):  
Cytochrome P450 ◽  
Protein Interactions ◽  
Hormone Receptors ◽  
Radioligand Binding ◽  
Cytochrome P450 Enzymes ◽  
Fatty Acid Derivatives ◽  
Affinity Constants ◽  
Cellular Lipids ◽  
Endogenous Substrates ◽  
The One

Most foreign compounds bind to one or more cytochrome P450 drug-metabolizing isozymes. These heme monooxygenases are most concentrated in the endoplasmic reticulum of liver cells but are present in virtually all biological membranes and in all cells. Some radioligands for known hormone receptors have been found to label, with comparable affinities, specific P450 enzymes. A characteristic feature of P450 enzymes is their broad and overlapping drug specificities, with affinity constants ranging over several orders of magnitude. Because fatty acid derivatives and steroids are endogenous substrates for the P450 enzymes, drugs may interfere with the generation of functional cellular lipids. The functional significance of high-affinity binding of drugs to the oxygenases may, on the one hand, be minimal and reflect extraneous or trivial drug–protein interactions. On the other hand, the drug–P450 union may in other cases mediate the major pharmacological response.Key words: cytochrome P450, radioligand binding, microsomes, sigma receptor, antiestrogen receptor.

The photochemistry of Ru(bpy)32+ in basic medium

1982 ◽  
Vol 60 (22) ◽  
pp. 2856-2858 ◽  
Author(s):  
Jin-Gou Xu ◽  
Gerald B. Porter
Keyword(s):  
Electron Transfer ◽  
Methyl Viologen ◽  
Reduction Product ◽  
Basic Medium ◽  
Electron Reduction ◽  
The One

Ru(bpy)32+ is photodecomposed in 0.3 M NaOH with [Formula: see text]. With methyl viologen also present, electron transfer quenching of the luminescence is accompanied by formation of the one electron reduction product of methyl viologen, MV+. The Ru(bpy)33+ formed in the corresponding oxidation is rapidly reduced by either OH− or MV+ to Ru(II).

Reactivity of the one-electron reduction product from nifedipine with relevant biological targets

1996 ◽  
Vol 101 (2) ◽  
pp. 89-101 ◽  
Author(s):  
Luis J. Núñez-Vergara ◽  
P.A. Navarrete-Encina ◽  
M.E. Ortiz ◽  
S. Bollo ◽  
J.A. Squella
Keyword(s):  
Reduction Product ◽  
Biological Targets ◽  
Electron Reduction ◽  
The One

scholarly journals High Spin Molecules: [Mn12O12(O2CCH2Cl)16(H2O)4] and the One-electron Reduction Product [PPh4][Mn12O12(O2CCH2Cl)16(H2O)3]

2000 ◽  
Vol 29 (4) ◽  
pp. 346-347 ◽  
Author(s):  
Hui-Lien Tsai ◽  
Tyn-Yih Jwo ◽  
Gene-Hsiang Lee ◽  
Yu Wang
Keyword(s):  
High Spin ◽  
Reduction Product ◽  
Electron Reduction ◽  
The One
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