000 | 01553 a2200445 4500 | ||
---|---|---|---|
005 | 20250514203828.0 | ||
264 | 0 | _c20041115 | |
008 | 200411s 0 0 eng d | ||
022 | _a0006-2960 | ||
024 | 7 |
_a10.1021/bi0488606 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aKlingen, Astrid R | |
245 | 0 | 0 |
_aNegatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins. _h[electronic resource] |
260 |
_bBiochemistry _cOct 2004 |
||
300 |
_a12383-9 p. _bdigital |
||
500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 |
_aAspartic Acid _xgenetics |
650 | 0 | 4 |
_aBurkholderia _xenzymology |
650 | 0 | 4 | _aCattle |
650 | 0 | 4 | _aComputer Simulation |
650 | 0 | 4 |
_aElectron Transport Complex III _xchemistry |
650 | 0 | 4 |
_aFerredoxins _xchemistry |
650 | 0 | 4 |
_aGlutamic Acid _xgenetics |
650 | 0 | 4 |
_aGlutamine _xgenetics |
650 | 0 | 4 |
_aHistidine _xchemistry |
650 | 0 | 4 | _aHydrogen Bonding |
650 | 0 | 4 | _aHydrogen-Ion Concentration |
650 | 0 | 4 |
_aIron-Sulfur Proteins _xchemistry |
650 | 0 | 4 | _aLigands |
650 | 0 | 4 | _aModels, Chemical |
650 | 0 | 4 | _aMutagenesis, Site-Directed |
650 | 0 | 4 |
_aRhodobacter sphaeroides _xenzymology |
650 | 0 | 4 | _aStatic Electricity |
650 | 0 | 4 | _aThermodynamics |
650 | 0 | 4 | _aTitrimetry |
700 | 1 | _aUllmann, G Matthias | |
773 | 0 |
_tBiochemistry _gvol. 43 _gno. 39 _gp. 12383-9 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi0488606 _zAvailable from publisher's website |
999 |
_c15142465 _d15142465 |