1.11.1.5	Ca2+	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	
1.11.1.5	Ca2+	pre-incubation with the cation has no effect on activity	659522	
1.11.1.5	Ca2+	with added Ca2+, the peroxidatic heme is five-coordinate high-spin and active	685251	
1.11.1.5	Fe	2 hemes	663999	
1.11.1.5	Fe	2 hemes per subunit	664002	
1.11.1.5	Fe	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	
1.11.1.5	Fe	two haeme groups	663918	
1.11.1.5	Fe	two haemes per monomer, pyridine haemochrome spectra	394632	
1.11.1.5	Fe2+	diheme cytochrome c peroxidase	724008	
1.11.1.5	Fe2+	heme	724658	
1.11.1.5	Iron	Fe(III) reduction to Fe(IV) in heme cofactor	725645	
1.11.1.5	Iron	heme	724372, 726385	
1.11.1.5	Iron	heme enzyme	725756	
1.11.1.5	Iron	heme iron Fe(III)	724337, 724463	
1.11.1.5	Iron	heme prosthetic group	394608, 394612, 394613, 394614, 394628, 394629	
1.11.1.5	additional information	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	
1.11.1.5	additional information	the enzyme is sensitive to increasing ionic strength	724335	
1.11.1.5	Na+	maximum turnover occurs at 50 mM NaCl	687825