. 1998 Jul 7;95(14):8020–8025. doi: 10.1073/pnas.95.14.8020

Table 1.

Visible absorption properties of several oxoferryl species and cytochrome c oxidase compounds P and F

Protein	λ_max (nm)/ ɛ(mM⁻¹ cm⁻¹)	λ_max (nm)/ ɛ(mM⁻¹ cm⁻¹)	Ref.
Protoheme/histidine axial ligation
Horseradish peroxidase	527/9.5	554/9.65	42
Prostaglandin synthase	527/10.1^*	557/9.3^*	43
Cytochrome c peroxidase	529/12.2^*	561/13.2^*	44
Arthromyces ramosus peroxidase	530/13.0^*	553/12.9^*	45
Lactoperoxidase	530^/9.8^	564^/9.0^	46
Myoglobin	549/9.8		47
Protoheme/tyrosinate axial ligation
Catalase	531^/8.8^	566^/9.6^	48
Protoheme/cysteinyl axial ligation
Cloroperoxodase	542/16.3^*	571/13.8^*	49
Modified protoheme/histidine axial ligation
Myeloperoxidase, pH 7		628/18	50
Myeloperoxidase, pH 11		635/25	50
Heme a/histidine axial ligation
Cytochrome c oxidase, P	≈565^†/≈7^†	≈605^†/≈15^†	21, 51
Cytochrome c oxidase, F		≈585^†/≈7^†	21, 51

Value estimated from the spectrum reported in the original paper.

^†

Values in the absolute absorption spectrum were estimated from the calculated difference spectrum in ref. 21 and the absolute spectrum of ferric heme a₃ in ref. 51.