| 000 | 01446 a2200397 4500 | ||
|---|---|---|---|
| 005 | 20250513063338.0 | ||
| 264 | 0 | _c19940526 | |
| 008 | 199405s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aUno, T | |
| 245 | 0 | 0 |
_aResonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centers. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cApr 1994 |
||
| 300 |
_a11912-20 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAlanine |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aCytochrome b Group |
| 650 | 0 | 4 |
_aCytochromes _xchemistry |
| 650 | 0 | 4 |
_aEscherichia coli _xmetabolism |
| 650 | 0 | 4 | _aEscherichia coli Proteins |
| 650 | 0 | 4 | _aHistidine |
| 650 | 0 | 4 | _aMacromolecular Substances |
| 650 | 0 | 4 | _aModels, Structural |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 | _aPoint Mutation |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aSpectroscopy, Fourier Transform Infrared _xmethods |
| 650 | 0 | 4 |
_aSpectrum Analysis, Raman _xmethods |
| 700 | 1 | _aMogi, T | |
| 700 | 1 | _aTsubaki, M | |
| 700 | 1 | _aNishimura, Y | |
| 700 | 1 | _aAnraku, Y | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 269 _gno. 16 _gp. 11912-20 |
|
| 999 |
_c8162810 _d8162810 |
||