The ferric haem g-factors
(for both low spin and high spin ferric haem forms)

This table comprises the reported values of g-factors of the high spin and low spin forms of haem iron in various proteins with various ligands. This is NOT a comprehensive database. One should note that differences in preparations as well as in accuracy of measurement, cause significant dispersion in g-factors reported for the same species. For example, entries 904, 905, 31, 35, 70, 93 refer obviously to the same EPR signal:
904 Bovine liver catalase; “catal3.spc”, major component 6.47 5.34 1.98 Data from our lab
905 BLC, pH8 exper with Martyn and Peter, alkaline (narrow) form 6.494 5.34 1.978 Data from our lab
31 Bovine liver catalase (BLC), Sigma; narrow signal, fraction ¼ 6.56 5.42 (Peisach, Blumberg et al. 1971)
35 BLC, Worthington; narrow signal, fraction ¼ 6.55 5.41 (Peisach, Blumberg et al. 1971)
70 Bovine liver catalase (Sigma); form A 6.5 5.37 1.98 (Williams-Smith and Patel 1975)
93 Bovine liver catalase; less rhombic (narrow); better seen at high pH 6.55 5.42 (Blum, Chance et al. 1978)

No. Sample g1 g2 g3 Reference
1 Horse erythrocyte catalase 6.6 5.4 2.03 (Torii & Ogura 1968)
2 Horse erythrocyte catalase - HF-complex 6.6 5.4 2.03 (Torii & Ogura 1968)
3 Horse erythrocyte catalase - HCN-complex 2.84 2.25 1.66 (Torii & Ogura 1968)
4 Horse erythrocyte catalase - HN3-complex; the high spin form 6.7 5.2 ? (Torii & Ogura 1968)
5 Horse erythrocyte catalase - HN3-complex; the low spin form 2.8 2.18 1.74 (Torii & Ogura 1968)
6 Horseradish peroxidase (FeIII); low pH 6.35 5.65 2 (Blumberg, Peisach et al. 1968)
7 Horseradish peroxidase (FeIII); high pH 2.9 2.1 1.6 (Blumberg, Peisach et al. 1968)
8 Horseradish peroxidase (FeIII); CN-complex 3.05 2.1 2.1 (Blumberg, Peisach et al. 1968)
9 Cyt-c-peroxidase (FeIII); low pH 6.4 5.6 2 (Wittenberg, Kampa et al. 1968)
10 Cyt-c-peroxidase (FeIII); high pH 2.6 2.2 1.9 (Wittenberg, Kampa et al. 1968)
11 Cyt-c-peroxidase (FeIII); CN-complex 3 2.1 - (Wittenberg, Kampa et al. 1968)
12 Nhis - Hb(d51/2) - -OH (O-type low spin methaemoglobin 2.55 2.17 1.85 (Blumberg & Peisach 1971)
13 Nhis - Hb(d51/2) -Nhis (H-type low spin methaemoglobin 2.8 2.26 1.67 (Blumberg & Peisach 1971)
14 Nhis - Hb(d51/2) - Smeth (C-type low spin methaemoglobin 3.15 2.25 1.25 (Blumberg & Peisach 1971)
15 Nhis - Hb(d51/2) - ? (B-type low spin methaemoglobin 2.95 2.26 1.47 (Blumberg & Peisach 1971)
16 Scys - Hb(d51/2) - H2O (P-type low spin methaemoglobin 2.41 2.25 1.93 (Blumberg & Peisach 1971)
17 sulfMb (FeIII) (pH 6); the high spin form 6 6 2 (Berzofsky, Peisach et al. 1971)
18 sulfMb (FeIII) (pH 6); the low spin form 2.5 2.26 1.83 (Berzofsky, Peisach et al. 1971)
19 sulfMb (FeIII) - OH- (pH 10-11) 2.44 2.2 1.88 (Berzofsky, Peisach et al. 1971)
20 Mb (FeIII) - OH- (pH 10-11) 2.6 2.15 1.83 (Berzofsky, Peisach et al. 1971)
21 sulfMb (FeIII) - N3- 2.61 2.23 1.8 (Berzofsky, Peisach et al. 1971)
22 Mb (FeIII) - N3- 2.82 2.19 1.71 (Berzofsky, Peisach et al. 1971)
23 sulfMb (FeIII) - CN- 2.65 2.43 1.65 (Berzofsky, Peisach et al. 1971)
24 Mb (FeIII) - CN- 3.5 1.9 <0.79 (Berzofsky, Peisach et al. 1971)
25 sulfMb (FeIII) - SH- (?) 2.38 2.26 1.91 (Berzofsky, Peisach et al. 1971)
26 Mb (FeIII) - SH- (?) 2.58 2.25 1.83 (Berzofsky, Peisach et al. 1971)
27 Ferric Mb (at zero crossing of the derivative) 5.92 5.92 - (Peisach, Blumberg et al. 1971)
28 Ferrihaemoglobin A (at zero crossing of the derivative) 5.89 5.89 - (Peisach, Blumberg et al. 1971)
29 Ferrimyoglobin fluoride (rhombicity 0.88%) 6.05 5.91 - (Peisach, Blumberg et al. 1971)
30 Human red blood cell catalase 6.7 5.4 - (Peisach, Blumberg et al. 1971)
31 Bovine liver catalase (BLC), Sigma; narrow signal, fraction ¼ 6.56 5.42 - (Peisach, Blumberg et al. 1971)
32 Bovine liver catalase (BLC), Sigma; broad signal, fraction ¾ 6.9 5.04 - (Peisach, Blumberg et al. 1971)
33 BLC, Sigma; sup.nat. after 37,000x30’; narrow signal, fraction ¼ 6.54 5.43 - (Peisach, Blumberg et al. 1971)
34 BLC, Sigma; sup.nat. after 37,000x30’; broad signal, fraction ¾ 6.93 5.12 - (Peisach, Blumberg et al. 1971)
35 BLC, Worthington; narrow signal, fraction ¼ 6.55 5.41 - (Peisach, Blumberg et al. 1971)
36 BLC, Worthington; broad signal, fraction ¾ 6.88 5.05 - (Peisach, Blumberg et al. 1971)
37 BLC, Worthington, concentrated; narrow signal, fraction ¼ 6.55 5.44 - (Peisach, Blumberg et al. 1971)
38 BLC, Worthington, concentrated; broad signal, fraction ¾ 6.88 5.05 - (Peisach, Blumberg et al. 1971)
39 BLC, Sigma, dialysed against water; narrow signal, fraction 4/4 6.63 5.4 - (Peisach, Blumberg et al. 1971)
40 BLC, Sigma, dialysed against water; broad signal, fraction 0/4 - - - (Peisach, Blumberg et al. 1971)
41 BLC, Worthington, BioGel P-2; narrow signal, fraction 4/4 6.51 5.41 - (Peisach, Blumberg et al. 1971)
42 BLC, Worthington, BioGel P-2; broad signal, fraction 0/4 - - - (Peisach, Blumberg et al. 1971)
43 BLC, Worthington, Chelex 100; narrow signal, fraction 0/4 - - - (Peisach, Blumberg et al. 1971)
44 BLC, Worthington, Chelex 100; broad signal, fraction 4/4 6.84 5.06 - (Peisach, Blumberg et al. 1971)
45 BLC, Worthington, plus KF; narrow signal, fraction 4/4 6.64 5.39 - (Peisach, Blumberg et al. 1971)
46 BLC, Worthington plus KF; broad signal, fraction 0/4 - - - (Peisach, Blumberg et al. 1971)
47 Catalase from Micrococcus lysodeikticus 6.2 5.8 - (Ehrenberg & Estabrook 1966)
48 Catalase from bacteria 6.5 5.45 - (Peisach, Blumberg et al. 1971)
49 Myeloperoxidase (MPO) purified from porcine neutrophils 6.78 5.12 - (Hatatanaka, Chiba et al. 1987)
50 Cyt b-558 of the NADPH oxidase in the stimulated state 6.47 5.49 - (Hatatanaka, Chiba et al. 1987)
51 MPO in pig granulocytes 7.02-7.03 5.20-5.22 1.94-1.96 (Fujii & Kakinuma 1992)
52 MPO in pig granulocytes, treated with KCN 2.84 2.17-2.24 1.61-1.66 (Fujii & Kakinuma 1992)
53 Eosinophil peroxidase (EPO) from pig granulocytes (L.s.) 2.86-2.87 2.13-2.21 1.66-1.67 (Fujii & Kakinuma 1992)
54 Eosinophil peroxidase (EPO) from pig granulocytes (H.s.) 6.86 5.23 1.96 (Fujii & Kakinuma 1992)
55 Cellular EPO (H.s.) 6.6 - - (ref 31) in (Fujii, 1992)
56 Purified EPO (H.s.) 6.5 - - (Bolscher, Plat et al. 1984)
57 Cyt b-558 of the NADPH oxidase 3.20±0.05 - - (Fujii & Kakinuma 1992)
58 Cyt b-558 of the NADPH oxidase 3.26 - - (Miki, Fujii et al. 1992)
59 Micrococcus lysodeikticus catalase 6.58 5.56 - (Benecky, Frew et al. 1993)
60 Micrococcus lysodeikticus catalase Compound I 3.44 - - (Benecky, Frew et al. 1993)
61 His93Tyr variant of horse heart myoglobin (mimicking catalase) 7.13 4.89 1.93 (Hildebr&, Burk et al. 1995)
62 His93Tyr variant of horse heart myoglobin (mimicking catalase 6.28 5.83 1.99 (Hildebr&, Burk et al. 1995)
63 Ascorbate peroxidase (with and without glycerol) 5.96-6.00 5.18-5.24 - (Patterson, Poulos et al. 1995)
64 p cation radical of ascorbate peroxidase Compound I 3.27 3.27 1.99 (Patterson, Poulos et al. 1995)
65 Catalase-peroxidase from Streptomyces sp. , H.s. (my interpr) 6.619 5.117 - (Youn, Yim et al. 1995)
66 Catalase-peroxidase from Streptomyces sp. H.s. (my interpr) 6.021 5.597 - (Youn, Yim et al. 1995)
67 Alpha chain, Hb A (d55/2) 6.18 5.78 - (Peisach, Blumberg et al. 1969)
68 Alpha chain, Hb A (d51/2) - -OH 2.56 2.18 1.88 (Peisach, Blumberg et al. 1969)
69 Alpha chain Hb(d51/2) -Nhis (dihistidyl form) 2.7 2.31 1.69 (Peisach, Blumberg et al. 1969)
70 Bovine liver catalase (Sigma); form A 6.5 5.37 1.98 (Williams-Smith & Patel 1975)
71 Bovine liver catalase (Sigma); form B 6.8 5.07 - (Williams-Smith & Patel 1975)
72 Bile pigment in bovine liver catalase (Sigma) 8.52 2.93 1.52 (Williams-Smith & Patel 1975)
73 Human erythrocyte catalase (water) 6.5 5.33 1.981 (Williams-Smith & Patel 1975)
74 Human erythrocyte catalase (formate) 6.78 5.09 1.959 (Williams-Smith & Patel 1975)
75 Human erythrocyte catalase (nitrite) 6.64 5.17 1.97 (Williams-Smith & Patel 1975)
76 Rat liver catalase (water) 6.5 5.35 1.982 (Williams-Smith & Patel 1975)
77 Rat liver catalase (formate) 6.8 5.11 1.954 (Williams-Smith & Patel 1975)
78 Rat liver catalase (nitrite) 6.65 5.2 1.973 (Williams-Smith & Patel 1975)
79 Bovine liver catalase (water) 6.5 5.37 1.979 (Williams-Smith & Patel 1975)
80 Bovine liver catalase (formate) 6.79 5.07 1.952 (Williams-Smith & Patel 1975)
81 Bovine liver catalase (nitrite) 6.67 5.18 1.97 (Williams-Smith & Patel 1975)
82 Bovine liver catalase (fluoride) 6.53 5.35 1.98 (Williams-Smith & Patel 1975)
83 Bovine liver catalase (azide) 6.59 5.32 - (Williams-Smith & Patel 1975)
84 Bovine liver catalase (azide; >0.2 M) 6.86 4.98 - (Williams-Smith & Patel 1975)
85 Bovine liver catalase (hypophosphite) 6.71 5.18 - (Williams-Smith & Patel 1975)
86 Bovine liver catalase (acetate) 6.8 5.08 - (Williams-Smith & Patel 1975)
87 Bovine liver catalase (in distilled water, not in any buffer) 6.8 5.09 - (Williams-Smith & Patel 1975)
88 Bovine liver catalase (in water, 24 h dialysis) 6.51 5.33 - (Williams-Smith & Patel 1975)
89 Catalase type A in rat liver 6.5 5.35 - (Williams-Smith & Morrison 1975)
90 Catalase type B in rat liver 6.8 5.07 - (Williams-Smith & Morrison 1975)
91 Catalase type A in human blood 6.49 5.35 - (Williams-Smith & Morrison 1975)
92 Bovine liver catalase; more rhombic (broad); better seen at low pH 6.9 5.05 - (Blum, Chance et al. 1978)
93 Bovine liver catalase; less rhombic (narrow); better seen at high pH 6.55 5.42 - (Blum, Chance et al. 1978)
94 Neurospora crassa catalase (narrow) 6.33 5.48 1.99 (Jacob & Orme-Johnson 1979)
95 Neurospora crassa catalase (broad) 6.62 5.18 1.99 (Jacob & Orme-Johnson 1979)
96 Neurospora crassa catalase + 0.9 mM NaN3 (the azide complex) 2.5 2.26 1.87 (Jacob & Orme-Johnson 1979)
97 Neurospora crassa catalase + 0.2 mM NaOCHO (the formate complex) 6.51 5.34 1.99 (Jacob & Orme-Johnson 1979)
98 Cytochrome c peroxidase (CcP) from bakers’ yeast (low spin) 2.7 2.2 1.78 (Yonetani & Anni 1987)
99 Cytochrome c peroxidase (CcP) from bakers’ yeast (high spin) 6.4 5.3 1.97 (Yonetani & Anni 1987)
100 Nhis - Hb(d51/2) - -OH Human metHb; pH6.4-8.9 2.59 2.17 1.83 (Levy, Kuppusamy et al. 1990)
101 Nhis - Hb(d51/2) -Nhis ; Human metHb; pH6.4-8.9 (B-complex) 2.83 2.26 1.63 (Levy, Kuppusamy et al. 1990)
102 Human metHb; pH6.4-8.9 (C-complex) - also histidine complex??? 2.98 2.28 - (Levy, Kuppusamy et al. 1990)
901 Human blood (intensive care) 6.48 5.32 1.98 Data from our lab, 1998
902 Neonatal pig blood, narrow signal 6.46 5.34 1.98 Data from our lab, 1998
903 Neonatal pig blood, broad signal 6.78 5.07 1.954 Data from our lab, 1998
904 BLC, pH7, "catal3.spc", major component ("alkaline") 6.47 5.34 1.98 Data from our lab, 1998
905 BLC, pH8 exper with Martyn and Peter, alkaline (narrow) form 6.494 5.34 1.978 Data from our lab, 1998
906 BLC, pH5.6, exper with Martyn and Peter, acidic (broad) form 6.807 5.047 1.952 Data from our lab, 1998
907 BLC, pH 6, "exper catal2" acidic (broad) form 6.709 5.17 1.965 Data from our lab, 1998
908 BLC, pH6.6, "haem prot 2 exper" acidic (broad) form 6.81 5.056 1.952 Data from our lab, 1998
909 BLC, pH7, "catal1.spc", minor component ("acidic") 6.62 5.19 1.97 Data from our lab, 1998
910 BLC-fluoride (pH7.5; "haem prot,2 exper") 6.552 5.375 1.981 Data from our lab, 1998
911 BLC-fluoride (pH7; exper with M and P) 6.554 5.362 1.979 Data from our lab, 1998
912 BLC-format (the same at pH5.6-7; exper with M and P) 6.804 5.043 1.952 Data from our lab, 1998
913 BLC-format "haem prot.2 exper", 6.807 5.04 1.952 Data from our lab, 1998
914 BLC + KNO2, pH 6, "exper catal2" 6.66 5.163 1.965 Data from our lab, 1998
915 BLC, pH7(?), "catal5.spc", + ONOO- 6.85 5 1.945 Data from our lab, 1998
916 HPII, pH6-8, "narrow", alkaline 6.576 5.315 1.974 Data from our lab, 1998
917 HPII, pH6-8, low spin I 2.427 2.305 1.858 Data from our lab, 1998
918 HPII, pH6-8, low spin II 2.399 2.286 1.897 Data from our lab, 1998
919 HPII-formate, pH6; exper "catal2" 6.673 5.215 1.966 Data from our lab, 1998
920 HN mutant, pH6, pH8 6.56 5.24 1.974 Data from our lab, 1998
921 HN mutant, pH8, pH6 6.55 5.41 1.974 Data from our lab, 1998
922 Aspergillus catalase, "narrow", alkaline, pH 8 6.457 5.371 1.981 Data from our lab, 1998
923 Aspergillus catalase, "broad", acidic, pH6.3 6.718 5.085 1.96 Data from our lab, 1998
924 Aspergillus catalase + 100 mM formate, pH6.3 6.821 5.02 1.951 Data from our lab, 1998
925 Bile pigment in BLC 8.45 2.96 Data from our lab, 1998
926 Bile pigment in BLC "haem prot 2 exper" acetate series 8.45 2.97 Data from our lab, 1998
927 Bile pigment in BLC "haem prot.2 exper", fluoride series 8.45 2.95 Data from our lab, 1998
928 Bile pigment in BLC "haem prot.2 exper", formate series 8.46 2.96 Data from our lab, 1998
929 Bile pigment in BLC "calat2", nitrite series 8.47 2.94 Data from our lab, 1998
930 Bile pigment in BLC+KNO2 "calat2", nitrite series 8.47 2.96 Data from our lab, 1998

REFERENCES

Benecky, M. J., J. E. Frew, et al. (1993). “Epr and Endor Detection of Compound-I From Micrococcus-Lysodeikticus Catalase.” Biochemistry 32(44): 11929-11933.

Berzofsky, J. A., J. Peisach, et al. (1971). “Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives.” Journal of Biological Chemistry 246(10): 3367-3377.

Blum, H., B. Chance, et al. (1978). “Effect of pH on bovine liver catalase as determined by electron paramagnetic resonance.” Biochimica et Biophysica Acta 534: 317-321.

Blumberg, W. E. and J. Peisach (1971). A unified theory for low spin forms of all ferric heme proteins as studied by EPR. Probes of structure and function of macromolecules and membranes. B. Chance, T. Yonetani and A. S. Mildvan. 2: 215-229.

Blumberg, W. E., J. Peisach, et al. (1968). “The Electron Structure of Protoheme Proteins. I. An Electron Paramagnetic Resonance and Optical Study of Horseradish Peroxidase and it's Derivatives.” Journal of Biological Chemistry 243(8): 1854-1862.

Bolscher, G. J. M., H. Plat, et al. (1984). “Some Properties of Human Eosinophil Peroxidase, a Comparison With Other Peroxidases.” Biochimica Et Biophysica Acta 784(2-3): 177-186.

Ehrenberg, A. and R. W. Estabrook (1966). Acta Chem. Scand. 20: 1667.

Fujii, H. and K. Kakinuma (1992). “Electron-Paramagnetic Resonance Studies On Cytochrome-B-558 and Peroxidases of Pig-Blood Granulocytes.” Biochimica Et Biophysica Acta 1136(3): 239-246.

Hatatanaka, A., T. Chiba, et al. (1987). “Electron-Spin-Resonance Signals From Stimulated and Resting Porcine Blood Neutrophils.” Febs Letters 214(2): 279-284.

Hildebrand, D. P., D. L. Burk, et al. (1995). “The Proximal Ligand Variant His93tyr of Horse Heart Myoglobin.” Biochemistry 34(6): 1997-2005.

Jacob, G. S. and W. H. Orme-Johnson (1979). “Catalase of Neurospora crassa. 2. Electron paramagnetic resonance and chemical properties of the prosthetic group.” Biochemistry 18(14): 2975-2980.

Levy, A., P. Kuppusamy, et al. (1990). “Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions.” Biochemistry 29(40): 9311-6.

Miki, T., H. Fujii, et al. (1992). “Epr Signals of Cytochrome-B558 Purified From Porcine Neutrophils.” Journal of Biological Chemistry 267(27): 19673-19675.

Patterson, W. R., T. L. Poulos, et al. (1995). “Identification of a Porphyrin Pi-Cation-Radical in Ascorbate Peroxidase Compound-I.” Biochemistry 34(13): 4342-4345.

Peisach, J., W. E. Blumberg, et al. (1971). “The effect of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance.” Journal of Biological Chemistry 246(10): 3342-3355.

Peisach, J., W. E. Blumberg, et al. (1969). “Hemoglobin A: an electron paramagnetic resonance study of the effects of interchain contacts on the heme symmetry of high-spin and low-spin derivatives of ferric alpha chains.” Proceedings of the National Academy of Sciences of the USA 63: 934-939.

Torii, K. and Y. Ogura (1968). “Studies on the EPR and light absorption spectra of horse erythrocyte catalase and its derivatives.” Journal of Biochemistry 64(2): 171-179.

Williams-Smith, D. L. and P. J. Morrison (1975). “Electron paramagnetic resonance spectra of catalase in mammalian tissues.” Biochim. Biophys. Acta 405: 253-261.

Williams-Smith, D. L. and K. Patel (1975). “Induced changes in the electron paramagnetic resonance spectra of mammalian catalases.” Biochim. Biophys. Acta 405: 243-252.

Wittenberg, B. A., L. Kampa, et al. (1968). “The Electron Structure of Protoheme Proteins. II. An Electron Paramagnetic Resonance and Optical Study of Cytochrome c Peroxidase and its Derivatives.” Journal of Biological Chemistry 243(8): 1863-1870.

Yonetani, T. and H. Anni (1987). “Yeast Cytochrome-c Peroxidase - Coordination and Spin States of Heme Prosthetic Group.” Journal of Biological Chemistry 262(20): 9547-9554.

Youn, H. D., Y. I. Yim, et al. (1995). “Spectral Characterization and Chemical Modification of Catalase- Peroxidase From Streptomyces Sp.” Journal of Biological Chemistry 270(23): 13740-13747.

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