Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster.-Reference-Cited by-同舟云学术

Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster.

Published:1983-09 Issue:18 Volume:258 Page:11157-11164
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Christner J A,Janick P A,Siegel L M,Münck E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Appendix: photochemical formation of deazaflavin dimers

2. Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and iron sulfide (Fe4S4) prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit

3. Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups.

4. Mössbauer evidence for exchange-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex.

5. Electron paramagnetic resonance and optical evidence for interaction between siroheme and the tetranuclear iron-sulfur center (Fe4S4) prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands

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