Tags

Type your tag names separated by a space and hit enter

Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.
Proc Natl Acad Sci U S A. 1989 Dec; 86(24):9846-50.PN

Abstract

Active beef heart aconitase contains an iron-sulfur cluster with an [Fe4S4]2+ core. This cluster can be converted into Fe3S4 with concomitant loss of enzymatic activity. We have reconstituted apo-aconitase with iron and selenide to obtain Fe4Se4 aconitase. The Se analog has higher catalytic activity than the native S-containing enzyme when isocitrate is the substrate. Oxidation of [Fe4Se4]2+ with ferricyanide yields the inactive [Fe3Se4]1+ form. The Se-containing 3-Fe cluster can be reduced to [Fe3Se4]0. We have studied the [Fe3S4]1+,0, [Fe3Se4]1+,0, and [Fe4Se4]2+ states with Mössbauer spectroscopy from 1.3 K to 200 K in magnetic fields up to 6.0 T. The spectra of the S- and Se-containing enzymes were found to be remarkably similar. The spectra of the 3-Fe clusters were analyzed and the salient features of the electronic structure are discussed.

Links

PMC Free PDF

Authors+Show Affiliations

Surerus KK
Gray Freshwater Biological Institute, University of Minnesota, Navarre 55392.
Kennedy MC
No affiliation info available
Beinert H
No affiliation info available
Münck E
No affiliation info available

MeSH

Aconitate HydrataseAnimalsCattleElectron Spin Resonance SpectroscopyIronIron-Sulfur ProteinsKineticsMetalloproteinsMyocardiumOxidation-ReductionSpectrum AnalysisSulfur

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

2557631

Citation

Surerus, K K., et al. "Mössbauer Study of the Inactive Fe3S4 and Fe3Se4 and the Active Fe4Se4 Forms of Beef Heart Aconitase." Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 24, 1989, pp. 9846-50.
Surerus KK, Kennedy MC, Beinert H, et al. Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase. Proc Natl Acad Sci U S A. 1989;86(24):9846-50.
Surerus, K. K., Kennedy, M. C., Beinert, H., & Münck, E. (1989). Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase. Proceedings of the National Academy of Sciences of the United States of America, 86(24), 9846-50.
Surerus KK, et al. Mössbauer Study of the Inactive Fe3S4 and Fe3Se4 and the Active Fe4Se4 Forms of Beef Heart Aconitase. Proc Natl Acad Sci U S A. 1989;86(24):9846-50. PubMed PMID: 2557631.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase. AU - Surerus,K K, AU - Kennedy,M C, AU - Beinert,H, AU - Münck,E, PY - 1989/12/1/pubmed PY - 1989/12/1/medline PY - 1989/12/1/entrez SP - 9846 EP - 50 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 86 IS - 24 N2 - Active beef heart aconitase contains an iron-sulfur cluster with an [Fe4S4]2+ core. This cluster can be converted into Fe3S4 with concomitant loss of enzymatic activity. We have reconstituted apo-aconitase with iron and selenide to obtain Fe4Se4 aconitase. The Se analog has higher catalytic activity than the native S-containing enzyme when isocitrate is the substrate. Oxidation of [Fe4Se4]2+ with ferricyanide yields the inactive [Fe3Se4]1+ form. The Se-containing 3-Fe cluster can be reduced to [Fe3Se4]0. We have studied the [Fe3S4]1+,0, [Fe3Se4]1+,0, and [Fe4Se4]2+ states with Mössbauer spectroscopy from 1.3 K to 200 K in magnetic fields up to 6.0 T. The spectra of the S- and Se-containing enzymes were found to be remarkably similar. The spectra of the 3-Fe clusters were analyzed and the salient features of the electronic structure are discussed. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/2557631/Mössbauer_study_of_the_inactive_Fe3S4_and_Fe3Se4_and_the_active_Fe4Se4_forms_of_beef_heart_aconitase_ DB - PRIME DP - Unbound Medicine ER -