Involvement of a labile axial histidine in coupling electron and proton transfer in Methylophilus methylotrophus cytochrome c"
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb17204.x/fullpdf
Reference21 articles.
1. Characterization and NMR studies of a novel cytochrome c isolated from Methylophilus methylotrophus which shows a redox-linked change of spin state
2. Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands
3. A theoretical model of the intensity of the near-infrared porphyrin-to-iron charge-transfer transitions in low-spin iron(III) haemoproteins. A correlation between the intensity of the magnetic circular dichroism bands and the rhombic distortion parameter of iron
4. Models of the cytochromes b. Control of axial ligand orientation with a hindered porphyrin system
5. Proton NMR and ESR studies of oxidized cytochrome c551 from Pseudomonas aeruginosa
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