The protein moiety modulates the redox potential in cytochromes c
- 23 January 1994
- Vol. 76 (6), 471-479
- https://doi.org/10.1016/0300-9084(94)90171-6
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Effects of Amino Acid Substitution on Three-Dimensional Structure: An X-Ray Analysis of Cytochrome c3, from Desulfovibrio vulgaris Hildenborough at 2 Å Resolution1The Journal of Biochemistry, 1991
- Sequence variability in bacterial cytochromes cBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
- The nirSTBM region coding for cytochrome cd1‐dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono‐, di‐, and tetraheme proteinsFEBS Letters, 1991
- S-Class Cytochromes c Have a Variety of Folding Patterns: Structure of Cytochrome c-553 from Desulfovibrio vulgaris Determined by the Multi-Wavelength Anomalous Dispersion Method1The Journal of Biochemistry, 1990
- Axial ligand replacement in horse heart cytochrome c by semisynthesisProteins-Structure Function and Bioinformatics, 1989
- Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.67 Å resolutionJournal of Molecular Biology, 1985
- The structure, function and evolution of cytochromesProgress in Biophysics and Molecular Biology, 1985
- Refined structure of cytochrome c3 at 1.8 Å resolutionJournal of Molecular Biology, 1984
- 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
- Structure and sequence of the multihaem cytochrome c3Nature, 1979