Table 1.
Biochemical and biophysical properties of the studied heme proteins
Overview of the respective redox potentials E°′ (Fe(III)/Fe(II)), amino acid composition, and overall secondary structure.
| Protein | Redox potential E°′ (Fe(II)/Fe(III)) | No. of amino acids (multimer) | Secondary structure elements (%) |
||
|---|---|---|---|---|---|
| β-Strands | Helix | Others | |||
| KpDyP | −350 ± 1 mV (26) | 299 (598) | 23.2 | 32.6 | 44 |
| NdCld | −113 ± 1 mV (30) | 264 (1320) | 26.9 | 42.0 | 31 |
| CCld | −126 ± 1.9 mV (31) | 182 (364) | 35.8 | 28.9 | 35.3 |
| hhMb | 28 ± 5 mV (32) | 154 (154) | 0 | 73.9 | 26.1 |
| AvTsdA | Heme 1 (His/Cys ligation): −185 mV (25) | 270 (270) | 4.8 | 39.5 | 55.7 |
| Heme 2 (His/Lys ligation): −129 mV (25) | |||||
| Heme 2 (His/Met ligation): +266 mV (25) | |||||
| LmChdC | −205 ± 3 mV (33) | 251 (1255) | 31 | 37.9 | 31 |