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421 related items for PubMed ID: 18646798
1. Structure and vibrational dynamics of model compounds of the [FeFe]-hydrogenase enzyme system via ultrafast two-dimensional infrared spectroscopy. Stewart AI, Clark IP, Towrie M, Ibrahim SK, Parker AW, Pickett CJ, Hunt NT. J Phys Chem B; 2008 Aug 14; 112(32):10023-32. PubMed ID: 18646798 [Abstract] [Full Text] [Related]
2. The role of CN and CO ligands in the vibrational relaxation dynamics of model compounds of the [FeFe]-hydrogenase enzyme. Kaziannis S, Wright JA, Candelaresi M, Kania R, Greetham GM, Parker AW, Pickett CJ, Hunt NT. Phys Chem Chem Phys; 2011 Jun 07; 13(21):10295-305. PubMed ID: 21537507 [Abstract] [Full Text] [Related]
3. Multiple-timescale photoreactivity of a model compound related to the active site of [FeFe]-hydrogenase. Ridley AR, Stewart AI, Adamczyk K, Ghosh HN, Kerkeni B, Guo ZX, Nibbering ET, Pickett CJ, Hunt NT. Inorg Chem; 2008 Sep 01; 47(17):7453-5. PubMed ID: 18665586 [Abstract] [Full Text] [Related]
4. Determination of the photolysis products of [FeFe]hydrogenase enzyme model systems using ultrafast multidimensional infrared spectroscopy. Stewart AI, Wright JA, Greetham GM, Kaziannis S, Santabarbara S, Towrie M, Parker AW, Pickett CJ, Hunt NT. Inorg Chem; 2010 Oct 18; 49(20):9563-73. PubMed ID: 20845922 [Abstract] [Full Text] [Related]
5. DFT/TDDFT exploration of the potential energy surfaces of the ground state and excited states of Fe2(S2C3H6)(CO)6: a simple functional model of the [FeFe] hydrogenase active site. Bertini L, Greco C, De Gioia L, Fantucci P. J Phys Chem A; 2009 May 14; 113(19):5657-70. PubMed ID: 19378958 [Abstract] [Full Text] [Related]
6. Influence of an electron-deficient bridging o-carborane on the electronic properties of an [FeFe] hydrogenase active site model. Schwartz L, Eriksson L, Lomoth R, Teixidor F, Viñas C, Ott S. Dalton Trans; 2008 May 14; (18):2379-81. PubMed ID: 18461189 [Abstract] [Full Text] [Related]
7. Refining the active site structure of iron-iron hydrogenase using computational infrared spectroscopy. Tye JW, Darensbourg MY, Hall MB. Inorg Chem; 2008 Apr 07; 47(7):2380-8. PubMed ID: 18307282 [Abstract] [Full Text] [Related]
8. Series of mixed valent Fe(II)Fe(I) complexes that model the Hox state of [FeFe]hydrogenase: redox properties, density-functional theory investigation, and reactivities with extrinsic CO. Thomas CM, Liu T, Hall MB, Darensbourg MY. Inorg Chem; 2008 Aug 04; 47(15):7009-24. PubMed ID: 18597449 [Abstract] [Full Text] [Related]
9. Vibrational cooling dynamics of a [FeFe]-hydrogenase mimic probed by time-resolved infrared spectroscopy. Caplins BW, Lomont JP, Nguyen SC, Harris CB. J Phys Chem A; 2014 Dec 11; 118(49):11529-40. PubMed ID: 25426927 [Abstract] [Full Text] [Related]
10. Theoretical studies of [FeFe]-hydrogenase: structure and infrared spectra of synthetic models. Zilberman S, Stiefel EI, Cohen MH, Car R. J Phys Chem B; 2006 Apr 06; 110(13):7049-57. PubMed ID: 16571021 [Abstract] [Full Text] [Related]
11. Time-resolved vibrational spectroscopy of [FeFe]-hydrogenase model compounds. Bingaman JL, Kohnhorst CL, Van Meter GA, McElroy BA, Rakowski EA, Caplins BW, Gutowski TA, Stromberg CJ, Webster CE, Heilweil EJ. J Phys Chem A; 2012 Jul 12; 116(27):7261-71. PubMed ID: 22612846 [Abstract] [Full Text] [Related]
12. Time-resolved infrared studies of a trimethylphosphine model derivative of [FeFe]-hydrogenase. Johnson M, Thuman J, Letterman RG, Stromberg CJ, Webster CE, Heilweil EJ. J Phys Chem B; 2013 Dec 12; 117(49):15792-803. PubMed ID: 24083980 [Abstract] [Full Text] [Related]
15. Computational definition of a mixed valent Fe(II)Fe(I) model of the [FeFe]hydrogenase active site resting state. Thomas CM, Darensbourg MY, Hall MB. J Inorg Biochem; 2007 Nov 12; 101(11-12):1752-7. PubMed ID: 17698202 [Abstract] [Full Text] [Related]
17. Targeting intermediates of [FeFe]-hydrogenase by CO and CN vibrational signatures. Yu L, Greco C, Bruschi M, Ryde U, De Gioia L, Reiher M. Inorg Chem; 2011 May 02; 50(9):3888-900. PubMed ID: 21443182 [Abstract] [Full Text] [Related]
18. Binuclear iron-sulfur complexes with bidentate phosphine ligands as active site models of Fe-hydrogenase and their catalytic proton reduction. Gao W, Ekström J, Liu J, Chen C, Eriksson L, Weng L, Akermark B, Sun L. Inorg Chem; 2007 Mar 19; 46(6):1981-91. PubMed ID: 17295467 [Abstract] [Full Text] [Related]