| 000 | 01905 a2200505 4500 | ||
|---|---|---|---|
| 005 | 20250517173156.0 | ||
| 264 | 0 | _c20180628 | |
| 008 | 201806s 0 0 eng d | ||
| 022 | _a1572-8773 | ||
| 024 | 7 |
_a10.1007/s10534-017-0050-x _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aBafana, Amit | |
| 245 | 0 | 0 |
_aStructural and functional characterization of mercuric reductase from Lysinibacillus sphaericus strain G1. _h[electronic resource] |
| 260 |
_bBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine _cOct 2017 |
||
| 300 |
_a809-819 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 |
_aBacillaceae _xchemistry |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 | _aBiocatalysis |
| 650 | 0 | 4 | _aBiodegradation, Environmental |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 |
_aEscherichia coli _xgenetics |
| 650 | 0 | 4 |
_aFlavin-Adenine Dinucleotide _xchemistry |
| 650 | 0 | 4 | _aGene Expression |
| 650 | 0 | 4 |
_aGenetic Vectors _xchemistry |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 |
_aMercury _xchemistry |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 |
_aNAD _xchemistry |
| 650 | 0 | 4 |
_aNADP _xchemistry |
| 650 | 0 | 4 |
_aOxidoreductases _xchemistry |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation, alpha-Helical |
| 650 | 0 | 4 | _aProtein Conformation, beta-Strand |
| 650 | 0 | 4 | _aProtein Interaction Domains and Motifs |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aKhan, Farha | |
| 700 | 1 | _aSuguna, Kaza | |
| 773 | 0 |
_tBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine _gvol. 30 _gno. 5 _gp. 809-819 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1007/s10534-017-0050-x _zAvailable from publisher's website |
| 999 |
_c27550005 _d27550005 |
||