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L C Seefeldt

Showing results (11-20 of 51) with videos related to

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Biochemistry|December 10, 1996
The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotidesM J Ryle, L C Seefeldt
The Journal of Biological Chemistry|December 15, 1987
Redox-dependent subunit dissociation of Azotobacter vinelandii hydrogenase in the presence of sodium dodecyl sulfateL C Seefeldt, D J Arp
Biochimie|January 1, 1986
Purification to homogeneity of Azotobacter vinelandii hydrogenase: a nickel and iron containing alpha beta dimerL C Seefeldt, D J Arp
The Journal of Biological Chemistry|February 14, 1997
Evidence for electron transfer-dependent formation of a nitrogenase iron protein-molybdenum-iron protein tight complex. The role of aspartate 39W N Lanzilotta, K Fisher, L C Seefeldt
The Journal of Biological Chemistry|August 19, 2000
Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenaseJ Christiansen, L C Seefeldt, D R Dean
Analytical Biochemistry|August 1, 1997
Entropies of redox reactions between proteins and mediators: the temperature dependence of reversible electrode potentials in aqueous buffersY Liu, L C Seefeldt, V D Parker
Analytical Biochemistry|November 18, 2000
Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteinsM Sørlie, L C Seefeldt, V D Parker
Biochemistry|June 4, 1996
Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complexW N Lanzilotta, K Fisher, L C Seefeldt
The Journal of Biological Chemistry|June 11, 1999
Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complexJ M Chan, M J Ryle, L C Seefeldt
Biochemistry|December 5, 1995
Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changesW N Lanzilotta, R C Holz, L C Seefeldt
Pageof 6

Showing results (11-20 of 51) with videos related to

Sort By:
Pageof 6
Biochemistry|December 10, 1996
The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotidesM J Ryle, L C Seefeldt
The Journal of Biological Chemistry|December 15, 1987
Redox-dependent subunit dissociation of Azotobacter vinelandii hydrogenase in the presence of sodium dodecyl sulfateL C Seefeldt, D J Arp
Biochimie|January 1, 1986
Purification to homogeneity of Azotobacter vinelandii hydrogenase: a nickel and iron containing alpha beta dimerL C Seefeldt, D J Arp
The Journal of Biological Chemistry|February 14, 1997
Evidence for electron transfer-dependent formation of a nitrogenase iron protein-molybdenum-iron protein tight complex. The role of aspartate 39W N Lanzilotta, K Fisher, L C Seefeldt
The Journal of Biological Chemistry|August 19, 2000
Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenaseJ Christiansen, L C Seefeldt, D R Dean
Analytical Biochemistry|August 1, 1997
Entropies of redox reactions between proteins and mediators: the temperature dependence of reversible electrode potentials in aqueous buffersY Liu, L C Seefeldt, V D Parker
Analytical Biochemistry|November 18, 2000
Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteinsM Sørlie, L C Seefeldt, V D Parker
Biochemistry|June 4, 1996
Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complexW N Lanzilotta, K Fisher, L C Seefeldt
The Journal of Biological Chemistry|June 11, 1999
Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complexJ M Chan, M J Ryle, L C Seefeldt
Biochemistry|December 5, 1995
Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changesW N Lanzilotta, R C Holz, L C Seefeldt
Pageof 6