Quick Search:

uzh logo
Browse by:
bullet
bullet
bullet
bullet

Zurich Open Repository and Archive

Maintenance: Tuesday, July the 26th 2016, 07:00-10:00

ZORA's new graphical user interface will be relaunched (For further infos watch out slideshow ZORA: Neues Look & Feel). There will be short interrupts on ZORA Service between 07:00am and 10:00 am. Please be patient.

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-48323

Kiger, L; Tilleman, L; Geuens, E; Hoogewijs, D; Lechauve, C; Moens, L; Dewilde, S; Marden, M C (2011). Electron transfer function versus oxygen delivery: a comparative study for several hexacoordinated globins across the animal kingdom. PLoS ONE, 6(6):e20478.

[img]
Preview
Published Version
Creative Commons: Attribution 4.0 International (CC BY 4.0)
PDF
1MB
View at publisher

Abstract

Caenorhabditis elegans globin GLB-26 (expressed from gene T22C1.2) has been studied in comparison with human neuroglobin (Ngb) and cytoglobin (Cygb) for its electron transfer properties. GLB-26 exhibits no reversible binding for O2 and a relatively low CO affinity compared to myoglobin-like globins. These differences arise from its mechanism of gaseous ligand binding since the heme iron of GLB-26 is strongly hexacoordinated in the absence of external ligands; the replacement of this internal ligand, probably the E7 distal histidine, is required before binding of CO or O2 as for Ngb and Cygb. Interestingly the ferrous bis-histidyl GLB-26 and Ngb, another strongly hexacoordinated globin, can transfer an electron to cytochrome c (Cyt-c) at a high bimolecular rate, comparable to those of inter-protein electron transfer in mitochondria. In addition, GLB-26 displays an unexpectedly rapid oxidation of the ferrous His-Fe-His complex without O2 actually binding to the iron atom, since the heme is oxidized by O2 faster than the time for distal histidine dissociation. These efficient mechanisms for electron transfer could indicate a family of hexacoordinated globin which are functionally different from that of pentacoordinated globins.

Citations

21 citations in Web of Science®
21 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

47 downloads since deposited on 09 Jun 2011
13 downloads since 12 months

Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology

04 Faculty of Medicine > Center for Integrative Human Physiology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2011
Deposited On:09 Jun 2011 10:52
Last Modified:04 Jul 2016 12:42
Publisher:Public Library of Science (PLoS)
ISSN:1932-6203
Funders:INSERM, DGA, University of Paris VI and XI, University of Antwerp, Fund for Scientific Research, Flanders
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1371/journal.pone.0020478
PubMed ID:21674044

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page