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Results 1 - 10 of 18 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Iron heme prosthetic group 394608, 394612, 394613, 394614, 394628, 394629
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Fe two haemes per monomer, pyridine haemochrome spectra 394632
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Ca2+ pre-incubation with the cation has no effect on activity 659522
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5more catalytic center activity increases with ionic strength in the case of cytochrome c551, with horse heart cytochrome c, the catalytic center activity decreases exponentially 659522
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Fe two haeme groups 663918
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Fe 2 hemes 663999
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Fe 2 hemes per subunit 664002
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Fe static titration of ferric cytochrome c peroxidase with reduced azurin shows that only one of the two hemes in the enzyme seems to be readily reduced 665456
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Ca2+ a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis 685208
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.5Ca2+ with added Ca2+, the peroxidatic heme is five-coordinate high-spin and active 685251
Results 1 - 10 of 18 > >>