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Mikhail Laryukhin

Showing results (1-10 of 13) with videos related to

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Journal of the American Chemical Society|September 14, 2006
Electron paramagnetic resonance studies of an integral membrane peptide inserted into aligned phospholipid bilayer nanotube arraysEthan S Karp, Johnson J Inbaraj, Mikhail Laryukhin, et al.
Biochemistry|July 22, 2014
Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediatesRoman Davydov, Mikhail Laryukhin, Amy Ledbetter-Rogers, et al.
Journal of the American Chemical Society|July 20, 2006
Determining the topology of integral membrane peptides using EPR spectroscopyJohnson J Inbaraj, Thomas B Cardon, Mikhail Laryukhin, et al.
Biochemistry|July 30, 2003
Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe proteinPaul M C Benton, Mikhail Laryukhin, Suzanne M Mayer, et al.
Journal of the American Chemical Society|September 15, 2005
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogenTran-Chin Yang, Nathan K Maeser, Mikhail Laryukhin, et al.
Journal of the American Chemical Society|May 8, 2003
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogenHong-In Lee, Paul M C Benton, Mikhail Laryukhin, et al.
Journal of the American Chemical Society|April 28, 2005
Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopyRobert Y Igarashi, Mikhail Laryukhin, Patricia C Dos Santos, et al.
Biochemistry|May 19, 2007
Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reductionBrett M Barney, Jammi McClead, Dmitriy Lukoyanov, et al.
Biochemistry|August 12, 2009
Trapping an intermediate of dinitrogen (N2) reduction on nitrogenaseBrett M Barney, Dmitriy Lukoyanov, Robert Y Igarashi, et al.
Inorganic Chemistry|November 22, 2007
Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environmentsDmitriy Lukoyanov, Vladimir Pelmenschikov, Nathan Maeser, et al.
Pageof 2

Showing results (1-10 of 13) with videos related to

Sort By:
Pageof 2
Journal of the American Chemical Society|September 14, 2006
Electron paramagnetic resonance studies of an integral membrane peptide inserted into aligned phospholipid bilayer nanotube arraysEthan S Karp, Johnson J Inbaraj, Mikhail Laryukhin, et al.
Biochemistry|July 22, 2014
Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediatesRoman Davydov, Mikhail Laryukhin, Amy Ledbetter-Rogers, et al.
Journal of the American Chemical Society|July 20, 2006
Determining the topology of integral membrane peptides using EPR spectroscopyJohnson J Inbaraj, Thomas B Cardon, Mikhail Laryukhin, et al.
Biochemistry|July 30, 2003
Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe proteinPaul M C Benton, Mikhail Laryukhin, Suzanne M Mayer, et al.
Journal of the American Chemical Society|September 15, 2005
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogenTran-Chin Yang, Nathan K Maeser, Mikhail Laryukhin, et al.
Journal of the American Chemical Society|May 8, 2003
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogenHong-In Lee, Paul M C Benton, Mikhail Laryukhin, et al.
Journal of the American Chemical Society|April 28, 2005
Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopyRobert Y Igarashi, Mikhail Laryukhin, Patricia C Dos Santos, et al.
Biochemistry|May 19, 2007
Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reductionBrett M Barney, Jammi McClead, Dmitriy Lukoyanov, et al.
Biochemistry|August 12, 2009
Trapping an intermediate of dinitrogen (N2) reduction on nitrogenaseBrett M Barney, Dmitriy Lukoyanov, Robert Y Igarashi, et al.
Inorganic Chemistry|November 22, 2007
Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environmentsDmitriy Lukoyanov, Vladimir Pelmenschikov, Nathan Maeser, et al.
Pageof 2