Energy of the low-lying excited levels for some reduced [4Fe4S] ferredoxins, from the relaxation broadening of the E.P.R. signals
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
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1. Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2019-05
2. Electron Magnetic Resonance of Iron–Sulfur Proteins in Electron-Transfer Chains: Resolving Complexity;Metals in Biology;2009-10-20
3. Electron spin relaxation enhancement measurements of interspin distances in human, porcine, and Rhodobacter electron transfer flavoprotein–ubiquinone oxidoreductase (ETF–QO);Journal of Magnetic Resonance;2008-02
4. Incorporation of either molybdenum or tungsten into formate dehydrogenase from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria;JBIC Journal of Biological Inorganic Chemistry;2003-12-11
5. Application of EPR Spectroscopy to the Structural and Functional Study of Iron-Sulfur Proteins;Advances in Inorganic Chemistry;1999
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