NDLI: Analysis of differences in oxygen sensitivity of Fe–S clusters

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Analysis of differences in oxygen sensitivity of Fe–S clusters

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Stiebritz, Martin T. Bruska, Marta K. Reiher, Markus
Description	Author Affiliation: Bruska MK ( ETH Zurich, Laboratorium für Physikalische Chemie, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland.)
Abstract	Many but not all iron–sulphur clusters in metalloproteins are known to be sensitive to molecular oxygen with dramatic consequences for their biological function. We performed a systematic quantum chemical investigation that sheds light on the differences in oxygen sensitivity depending on charge and spin states of these clusters as well as on their spatial fixation by the enzyme's scaffold. We find that significant structural distortions are required to bind $O_{2}$ exothermically to $[Fe_{2}S_{2}]$ and $[Fe_{3}S_{4}]$ clusters, while only small conformational changes allow for the thermodynamically favorable coordination of molecular oxygen to $[Fe_{4}S_{4}]$ cubanes and $[Fe_{4}S_{3}]$ clusters.
ISSN	14779226
Issue Number	24
Volume Number	42
e-ISSN	13645447
Journal	Dalton Trans.
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2013-06-28
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Iron-Sulfur Proteins Chemistry Oxygen Methods Enzymes Hydrogen Bonding Iron Metalloproteins Oxidation-Reduction Oxidative Stress Protein Binding Protein Conformation Spectrum Analysis Sulfur Temperature Thermodynamics Journal Article
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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