검색결과 : 8건
No. | Article |
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1 |
Resolution of Key Roles for the Distal Pocket Histidine in Cytochrome c Nitrite Reductases Lockwood CWJ, Burlat B, Cheesman MR, Kern M, Simon J, Clarke TA, Richardson DJ, Butt JN Journal of the American Chemical Society, 137(8), 3059, 2015 |
2 |
DFT Investigation of the Molybdenum Cofactor in Periplasmic Nitrate Reductases: Structure of the Mo(V) EPR-Active Species Biaso F, Burlat B, Guigliarelli B Inorganic Chemistry, 51(6), 3409, 2012 |
3 |
Original Design of an Oxygen-Tolerant [NiFe] Hydrogenase: Major Effect of a Valine-to-Cysteine Mutation near the Active Site Liebgott PP, de Lacey AL, Burlat B, Cournac L, Richaud P, Brugna M, Fernandez VM, Guigliarelli B, Rousset M, Leger C, Dementin S Journal of the American Chemical Society, 133(4), 986, 2011 |
4 |
Rates of Intra- and Intermolecular Electron Transfers in Hydrogenase Deduced from Steady-State Activity Measurements Dementin S, Burlat B, Fourmond V, Leroux F, Liebgott PP, Abou Hamdan A, Leger C, Rousset M, Guigliarelli B, Bertrand P Journal of the American Chemical Society, 133(26), 10211, 2011 |
5 |
Is engineering O-2-tolerant hydrogenases just a matter of reproducing the active sites of the naturally occurring O-2-resistant enzymes? Leroux F, Liebgott PP, Cournac L, Richaud P, Kpebe A, Burlat B, Guigliarelli B, Bertrand P, Leger C, Rousset M, Dementin S International Journal of Hydrogen Energy, 35(19), 10770, 2010 |
6 |
Introduction of Methionines in the Gas Channel Makes [NiFe] Hydrogenase Aero-Tolerant Dementin S, Leroux F, Cournac L, de Lacey AL, Volbeda A, Leger C, Burlat B, Martinez N, Champ S, Martin L, Sanganas O, Haumann M, Fernandez VM, Guigliarelli B, Fontecilla-Camps JC, Rousset M Journal of the American Chemical Society, 131(29), 10156, 2009 |
7 |
Characterization of two 2[4Fe4S] ferredoxins from Clostridium acetobutylicum Guerrini O, Burlat B, Leger C, Guigliarelli B, Soucaille P, Girbal L Current Microbiology, 56(3), 261, 2008 |
8 |
Major Mo(V) EPR Signature of Rhodobacter sphaeroides Periplasmic Nitrate Reductase Arising from a Dead-End Species That Activates upon Reduction. Relation to Other Molybdoenzymes from the DMSO Reductase Family Fourmond V, Burlat B, Dementin S, Arnoux P, Sabaty M, Boiry S, Guigliarelli B, Bertrand P, Pignol D, Leger C Journal of Physical Chemistry B, 112(48), 15478, 2008 |