| 000 | 01648 a2200457 4500 | ||
|---|---|---|---|
| 005 | 20250516184454.0 | ||
| 264 | 0 | _c20140320 | |
| 008 | 201403s 0 0 eng d | ||
| 022 | _a0006-3002 | ||
| 024 | 7 |
_a10.1016/j.bbabio.2013.11.016 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aSánchez-Azqueta, Ana | |
| 245 | 0 | 0 |
_aExternal loops at the ferredoxin-NADP(+) reductase protein-partner binding cavity contribute to substrates allocation. _h[electronic resource] |
| 260 |
_bBiochimica et biophysica acta _cFeb 2014 |
||
| 300 |
_a296-305 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAnabaena _xenzymology |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aBiocatalysis |
| 650 | 0 | 4 |
_aCoenzymes _xmetabolism |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aElectron Transport |
| 650 | 0 | 4 |
_aFerredoxin-NADP Reductase _xchemistry |
| 650 | 0 | 4 |
_aFerredoxins _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aMutant Proteins _xmetabolism |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aSpectrophotometry, Ultraviolet |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aMartínez-Júlvez, Marta | |
| 700 | 1 | _aHervás, Manuel | |
| 700 | 1 | _aNavarro, José A | |
| 700 | 1 | _aMedina, Milagros | |
| 773 | 0 |
_tBiochimica et biophysica acta _gvol. 1837 _gno. 2 _gp. 296-305 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.bbabio.2013.11.016 _zAvailable from publisher's website |
| 999 |
_c23351457 _d23351457 |
||