A Multi-Frequency Pulse EPR and ENDOR Approach to Study Strongly Coupled Nuclei in Frozen Solutions of High-Spin Ferric Heme Proteins

2008 ◽  
Vol 112 (12) ◽  
pp. 3859-3870 ◽  
Author(s):  
M. Fittipaldi ◽  
I. García-Rubio ◽  
F. Trandafir ◽  
I. Gromov ◽  
A. Schweiger ◽  
...  
Keyword(s):  
High Spin ◽  
Heme Proteins ◽  
Strongly Coupled ◽  
Pulse Epr ◽  
Ferric Heme ◽  
Frozen Solutions ◽  
Frequency Pulse

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

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.

A Soret Marker Band for Four-Coordinate Ferric Heme Proteins from Absorption Spectra of Isolated Fe(III)-Heme+and Fe(III)-Heme+(His) Ions in Vacuo

2008 ◽  
Vol 130 (36) ◽  
pp. 11856-11857 ◽  
Author(s):  
Morten Køcks Lykkegaard ◽  
Anneli Ehlerding ◽  
Preben Hvelplund ◽  
Umesh Kadhane ◽  
Maj-Britt Suhr Kirketerp ◽  
...  
Keyword(s):  
Absorption Spectra ◽  
Heme Proteins ◽  
Marker Band ◽  
Ferric Heme
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