Synthetic Models of the Active Site of Cytochrome P-450. 1st Communication. The Synthesis of a Doubly-Bridged Iron(II)-Porphyrin Carrying a Tightly Bound Thiolate Ligand

1987 ◽  
Vol 70 (4) ◽  
pp. 1173-1193 ◽  
Author(s):  
Beat Stäubli ◽  
Heinz Fretz ◽  
Umberto Piantini ◽  
Wolf-Dietrich Woggon
Keyword(s):  
Active Site ◽  
Thiolate Ligand ◽  
Cytochrome P 450 ◽  
Synthetic Models

scholarly journals Valence tautomerism in synthetic models of cytochrome P450

2016 ◽  
Vol 113 (24) ◽  
pp. 6611-6616 ◽  
Author(s):  
Pradip Kumar Das ◽  
Subhra Samanta ◽  
Ashley B. McQuarters ◽  
Nicolai Lehnert ◽  
Abhishek Dey
Keyword(s):  
Ground State ◽  
Active Site ◽  
Room Temperature ◽  
Thiyl Radical ◽  
Valence Tautomerism ◽  
Thiolate Ligand ◽  
Organic Solutions ◽  
Valence Tautomer ◽  
Heme Cofactor ◽  
Synthetic Models

CytP450s have a cysteine-bound heme cofactor that, in its as-isolated resting (oxidized) form, can be conclusively described as a ferric thiolate species. Unlike the native enzyme, most synthetic thiolate-bound ferric porphyrins are unstable in air unless the axial thiolate ligand is sterically protected. Spectroscopic investigations on a series of synthetic mimics of cytP450 indicate that a thiolate-bound ferric porphyrin coexists in organic solutions at room temperature (RT) with a thiyl-radical bound ferrous porphyrin, i.e., its valence tautomer. The ferric thiolate state is favored by greater enthalpy and is air stable. The ferrous thiyl state is favored by entropy, populates at RT, and degrades in air. These ground states can be reversibly interchanged at RT by the addition or removal of water to the apolar medium. It is concluded that hydrogen bonding and local electrostatics protect the resting oxidized cytP450 active site from degradation in air by stabilizing the ferric thiolate ground state in contrast to its synthetic analogs.

scholarly journals The cytochrome P-450 active site. Regiospecificity of prosthetic heme alkylation by olefins and acetylenes.

1983 ◽  
Vol 258 (7) ◽  
pp. 4202-4207 ◽  
Author(s):  
K L Kunze ◽  
B L Mangold ◽  
C Wheeler ◽  
H S Beilan ◽  
P R Ortiz de Montellano
Keyword(s):  
Active Site ◽  
Cytochrome P 450

The Topology of the Mammalian Cytochrome P-450 Active Site

1986 ◽  
pp. 77-88 ◽  
Author(s):  
Gerald T. Miwa ◽  
Anthony Y. H. Lu
Keyword(s):  
Active Site ◽  
Cytochrome P 450

Synthetic models for the active site of hemocyanin

1989 ◽  
Vol 36 (3-4) ◽  
pp. 327
Author(s):  
T.N. Sorrell ◽  
M.L. Garrity ◽  
J.R. Richards ◽  
V.A. Vankai
Keyword(s):  
Active Site ◽  
Synthetic Models

The active site of cytochrome P-450 nifedipine oxidase: a model-building study

1989 ◽  
Vol 7 (4) ◽  
pp. 206-211 ◽  
Author(s):  
Gyorgy G. Ferenczy ◽  
Garrett M. Morris
Keyword(s):  
Active Site ◽  
Model Building ◽  
Cytochrome P 450

Synthetic Models of the Active Site of Catechol Oxidase: Mechanistic Studies

ChemInform ◽  
2006 ◽  
Vol 37 (48) ◽  
Author(s):  
Iryna A. Koval ◽  
Patrick Gamez ◽  
Catherine Belle ◽  
Katalin Selmeczi ◽  
Jan Reedijk
Keyword(s):  
Active Site ◽  
Catechol Oxidase ◽  
Mechanistic Studies ◽  
Synthetic Models
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