| 000 | 01262 a2200337 4500 | ||
|---|---|---|---|
| 005 | 20250513063338.0 | ||
| 264 | 0 | _c19940526 | |
| 008 | 199405s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aArciero, D M | |
| 245 | 0 | 0 |
_aA di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cApr 1994 |
||
| 300 |
_a11878-86 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S. | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aChromatography, High Pressure Liquid |
| 650 | 0 | 4 |
_aCytochrome-c Peroxidase _xchemistry |
| 650 | 0 | 4 | _aElectron Spin Resonance Spectroscopy |
| 650 | 0 | 4 | _aElectrophoresis, Disc |
| 650 | 0 | 4 |
_aHeme _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aNitrosomonas _xenzymology |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSpectrophotometry |
| 700 | 1 | _aHooper, A B | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 269 _gno. 16 _gp. 11878-86 |
|
| 999 |
_c8162809 _d8162809 |
||