EPR potentiometric titration of c3-type cytochromes
- 1 June 1985
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 829 (2) , 262-267
- https://doi.org/10.1016/0167-4838(85)90196-7
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- The physics of hemoglobinPublished by Springer Nature ,2008
- NMR studies of electron transfer mechanisms in a protein with interacting redox centres: Desulfovibrio gigas cytochrome c3European Journal of Biochemistry, 1984
- Correlations studies between structural and redox properties of cytochromes C3Biochemical and Biophysical Research Communications, 1984
- ESR studies of cytochrome c3 from Desulfovibrio desulfuricans strain Norway 4Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Purification and characterization of cytochrome C3 (Mr 26,000) isolated from Desulfovibriodesulfuricans Norway strainBiochemical and Biophysical Research Communications, 1982
- The primary structure of the tetrahaem cytochrome from Desulfovibrio desulfuricans (strain norway 4). Description of a new class of low-potential cytochromeBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Current—potential responses for a tetrahemic protein: a method of determining the individual half-wave potentials of cytochrome c3 from desulfovibrio desulfuricans strain NorwayElectrochimica Acta, 1981
- Reversible voltammetric response for a molecule containing four non-equivalent redox sites with application to cytochrome c3 of Desulfovibrio vulgaris, strain MiyazakiJournal of Electroanalytical Chemistry and Interfacial Electrochemistry, 1980
- Oxidation-reduction potentials of the hemes in cytochrome c3 from Desulfovibrio gigas in the presence and absence of ferredoxin by EPR spectroscopyBiochimie, 1979
- EPR determination of the oxidation-reduction potentials of the hemes in cytochrome c3 from Desulfovibrio vulgarisBiochimie, 1978