Advanced

Studies of Ferric Heme Proteins with Highly Anisotropic/Highly Axial Low Spin (S=1/2) Electron Paramagnetic Resonance Signals with bis-Histidine and Histidine-Methionine Axial Iron Coordination

Zoppellaro, Giorgio; Bren, Kara L.; Ensign, Amy A.; Harbitz, Espen; Kaur, Ravinder; Hersleth, Hans-Petter; Ryde, Ulf LU ; Hederstedt, Lars LU and Andersson, K. Kristoffer (2009) In Biopolymers 91(12). p.1064-1082
Abstract
Six-coordinated heme groups are involved in a large variety of electron transfer reactions because of their ability to exist in both the ferrous (Fe2+) andferric (Fe3+) state without any large differences in structure. Our studies on hemes coordinated by two histidines (bis-His) and hemes coordinated by histidine and methionine (His-Met) will be reviewed. In both of these coordination environments, the heme core can exhibit ferric low spin (electron paramagnetic resonance EPR) signals with large g(max) values (also called Type I, highly anisotropic low spin, or highly axial low spin, HALS species) as Well as rhombic EPR (Type II) signals. In bis-His coordinated hemes rhombic and HALS envelopes are related to the orientation of the His... (More)
Six-coordinated heme groups are involved in a large variety of electron transfer reactions because of their ability to exist in both the ferrous (Fe2+) andferric (Fe3+) state without any large differences in structure. Our studies on hemes coordinated by two histidines (bis-His) and hemes coordinated by histidine and methionine (His-Met) will be reviewed. In both of these coordination environments, the heme core can exhibit ferric low spin (electron paramagnetic resonance EPR) signals with large g(max) values (also called Type I, highly anisotropic low spin, or highly axial low spin, HALS species) as Well as rhombic EPR (Type II) signals. In bis-His coordinated hemes rhombic and HALS envelopes are related to the orientation of the His groups with respect to each other such that (i) parallel His planes results in a rhombic signal and (ii) perpendicular His planes results in a HALS signal. Correlation between the structure of the heme and its ligands for heme with His-Met axial ligation and ligand-field parameters, as derived from a large series of cytochrome c variants, show, however, that for such a combination of axial ligands there is no clear-cut difference between the large g(max) and the "small ganisotropy" cases as a result of the relative Met-His arrangements. Nonetheless, a new linear correlation links the average shift <delta > of the heme methyl groups with the g(max) values. (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 1064-1082, 2009. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
H-1 NMR, EPR, cytochrome, DFT calculation, ligand-field anisotropy
in
Biopolymers
volume
91
issue
12
pages
1064 - 1082
publisher
John Wiley & Sons
external identifiers
  • wos:000270961600011
  • scopus:71749110766
ISSN
0006-3525
DOI
10.1002/bip.21267
language
English
LU publication?
yes
id
6ffb78a5-90d9-4615-9e61-53ffcadb9087 (old id 1507103)
date added to LUP
2009-11-23 10:14:48
date last changed
2017-09-03 03:49:33
@article{6ffb78a5-90d9-4615-9e61-53ffcadb9087,
  abstract     = {Six-coordinated heme groups are involved in a large variety of electron transfer reactions because of their ability to exist in both the ferrous (Fe2+) andferric (Fe3+) state without any large differences in structure. Our studies on hemes coordinated by two histidines (bis-His) and hemes coordinated by histidine and methionine (His-Met) will be reviewed. In both of these coordination environments, the heme core can exhibit ferric low spin (electron paramagnetic resonance EPR) signals with large g(max) values (also called Type I, highly anisotropic low spin, or highly axial low spin, HALS species) as Well as rhombic EPR (Type II) signals. In bis-His coordinated hemes rhombic and HALS envelopes are related to the orientation of the His groups with respect to each other such that (i) parallel His planes results in a rhombic signal and (ii) perpendicular His planes results in a HALS signal. Correlation between the structure of the heme and its ligands for heme with His-Met axial ligation and ligand-field parameters, as derived from a large series of cytochrome c variants, show, however, that for such a combination of axial ligands there is no clear-cut difference between the large g(max) and the "small ganisotropy" cases as a result of the relative Met-His arrangements. Nonetheless, a new linear correlation links the average shift &lt;delta &gt; of the heme methyl groups with the g(max) values. (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 1064-1082, 2009.},
  author       = {Zoppellaro, Giorgio and Bren, Kara L. and Ensign, Amy A. and Harbitz, Espen and Kaur, Ravinder and Hersleth, Hans-Petter and Ryde, Ulf and Hederstedt, Lars and Andersson, K. Kristoffer},
  issn         = {0006-3525},
  keyword      = {H-1 NMR,EPR,cytochrome,DFT calculation,ligand-field anisotropy},
  language     = {eng},
  number       = {12},
  pages        = {1064--1082},
  publisher    = {John Wiley & Sons},
  series       = {Biopolymers},
  title        = {Studies of Ferric Heme Proteins with Highly Anisotropic/Highly Axial Low Spin (S=1/2) Electron Paramagnetic Resonance Signals with bis-Histidine and Histidine-Methionine Axial Iron Coordination},
  url          = {http://dx.doi.org/10.1002/bip.21267},
  volume       = {91},
  year         = {2009},
}