Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

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

In English

Författare

  • Giorgio Zoppellaro
  • Kara L. Bren
  • Amy A. Ensign
  • Espen Harbitz
  • Ravinder Kaur
  • Hans-Petter Hersleth
  • Ulf Ryde
  • Lars Hederstedt
  • K. Kristoffer Andersson

Summary, in English

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.

Publiceringsår

2009

Språk

Engelska

Sidor

1064-1082

Publikation/Tidskrift/Serie

Biopolymers

Volym

91

Issue

12

Dokumenttyp

Artikel i tidskrift

Förlag

John Wiley & Sons Inc.

Ämne

  • Biological Sciences
  • Theoretical Chemistry

Nyckelord

  • H-1 NMR
  • EPR
  • cytochrome
  • DFT calculation
  • ligand-field anisotropy

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0006-3525