| 000 | 01777 a2200517 4500 | ||
|---|---|---|---|
| 005 | 20250514225035.0 | ||
| 264 | 0 | _c20050719 | |
| 008 | 200507s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 024 | 7 |
_a10.1074/jbc.C500171200 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aLin, Po-Chi | |
| 245 | 0 | 0 |
_aA vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cJun 2005 |
||
| 300 |
_a22560-3 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Motifs |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCircular Dichroism |
| 650 | 0 | 4 |
_aCysteine _xchemistry |
| 650 | 0 | 4 |
_aFerredoxins _xchemistry |
| 650 | 0 | 4 |
_aIron-Sulfur Proteins _xchemistry |
| 650 | 0 | 4 | _aMagnetics |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 | _aOxygen Consumption |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 |
_aQuinone Reductases _xchemistry |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 |
_aSodium _xchemistry |
| 650 | 0 | 4 |
_aSodium-Potassium-Exchanging ATPase _xchemistry |
| 650 | 0 | 4 |
_aSpectroscopy, Mossbauer _xmethods |
| 650 | 0 | 4 | _aUltraviolet Rays |
| 650 | 0 | 4 | _aVertebrates |
| 650 | 0 | 4 |
_aVibrio cholerae _xenzymology |
| 700 | 1 | _aPuhar, Andrea | |
| 700 | 1 | _aTürk, Karin | |
| 700 | 1 | _aPiligkos, Stergios | |
| 700 | 1 | _aBill, Eckhard | |
| 700 | 1 | _aNeese, Frank | |
| 700 | 1 | _aSteuber, Julia | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 280 _gno. 24 _gp. 22560-3 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.C500171200 _zAvailable from publisher's website |
| 999 |
_c15536172 _d15536172 |
||