Mechanistic origin of the correlation between spin state and spectra of model cytochrome P450 ferric heme proteins

1993 ◽  
Vol 115 (13) ◽  
pp. 5799-5802 ◽  
Author(s):  
Danni Harris ◽  
Gilda Loew
Keyword(s):  
Cytochrome P450 ◽  
Spin State ◽  
Heme Proteins ◽  
Ferric Heme

Drug metabolism, cytochrome P450 spin state, and phospholipid changes during pregnancy in the rat

1981 ◽  
Vol 30 (11) ◽  
pp. 1223-1225 ◽  
Author(s):  
R.G. Turcan ◽  
P.P. Tamburini ◽  
G.G. Gibson ◽  
D.V. Parke ◽  
A.M. Symons
Keyword(s):  
Cytochrome P450 ◽  
Drug Metabolism ◽  
Spin State

scholarly journals Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies

2020 ◽  
Vol 117 (36) ◽  
pp. 21914-21920 ◽  
Author(s):  
Camila Bacellar ◽  
Dominik Kinschel ◽  
Giulia F. Mancini ◽  
Rebecca A. Ingle ◽  
Jérémy Rouxel ◽  
...  
Keyword(s):  
Heme Proteins ◽  
Thermal Relaxation ◽  
Major Protein ◽  
Edge Structure ◽  
X Ray ◽  
Electron Transfer Protein ◽  
Cyt C ◽  
Ferric Heme ◽  
Function Relationship ◽  
X Ray Absorption

The structure–function relationship is at the heart of biology, and major protein deformations are correlated to specific functions. For ferrous heme proteins, doming is associated with the respiratory function in hemoglobin and myoglobins. Cytochromec(Cyt c) has evolved to become an important electron-transfer protein in humans. In its ferrous form, it undergoes ligand release and doming upon photoexcitation, but its ferric form does not release the distal ligand, while the return to the ground state has been attributed to thermal relaxation. Here, by combining femtosecond Fe Kαand KβX-ray emission spectroscopy (XES) with Fe K-edge X-ray absorption near-edge structure (XANES), we demonstrate that the photocycle of ferric Cyt c is entirely due to a cascade among excited spin states of the iron ion, causing the ferric heme to undergo doming, which we identify. We also argue that this pattern is common to a wide diversity of ferric heme proteins, raising the question of the biological relevance of doming in such proteins.

Studying high-spin ferric heme proteins by pulsed EPR spectroscopy: Analysis of the ferric form of the E7Q mutant of human neuroglobin

2007 ◽  
Vol 31 (3-4) ◽  
pp. 553-572 ◽  
Author(s):  
F. Trandafir ◽  
P. Heerdt ◽  
M. Fittipaldi ◽  
E. Vinck ◽  
S. Dewilde ◽  
...  
Keyword(s):  
High Spin ◽  
Epr Spectroscopy ◽  
Heme Proteins ◽  
Spectroscopy Analysis ◽  
Pulsed Epr ◽  
Ferric Heme

Kinetics of hepatic cytochrome P-450 reduction: correlation with spin state of the ferric heme

Biochemistry ◽  
1982 ◽  
Vol 21 (6) ◽  
pp. 1324-1330 ◽  
Author(s):  
Wayne L. Backes ◽  
Stephen G. Sligar ◽  
John B. Schenkman
Keyword(s):  
Spin State ◽  
Ferric Heme ◽  
Kinetics Of ◽  
Cytochrome P 450 ◽  
Hepatic Cytochrome
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