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D R Dean

Showing results (31-40 of 66) with videos related to

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Biochemistry|April 19, 1994
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene productL Zheng, R H White, V L Cash, et al.
Journal of Inorganic Biochemistry|September 23, 2000
The role of the MoFe protein alpha-125Phe and beta-125Phe residues in Azotobacter vinelandii MoFe protein-Fe protein interactionJ Christiansen, J M Chan, L C Seefeldt, et al.
The Journal of Biological Chemistry|February 7, 2001
Isolation and characterization of an acetylene-resistant nitrogenaseJ Christiansen, V L Cash, L C Seefeldt, et al.
Biochemistry|June 14, 2000
Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysisJ M Chan, W Wu, D R Dean, et al.
Biochemistry|August 12, 1998
Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenaseW N Lanzilotta, J Christiansen, D R Dean, et al.
The Journal of Biological Chemistry|November 10, 1995
Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe proteinJ W Peters, K Fisher, W E Newton, et al.
The Journal of Biological Chemistry|May 28, 1998
Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandiiL Zheng, V L Cash, D H Flint, et al.
The Journal of Biological Chemistry|March 3, 1995
Characteristics of NIFNE in Azotobacter vinelandii strains. Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenaseJ T Roll, V K Shah, D R Dean, et al.
The Journal of Biological Chemistry|April 5, 1992
Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interactionL C Seefeldt, T V Morgan, D R Dean, et al.
Journal of Bacteriology|April 1, 1987
Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifKK E Brigle, M C Weiss, W E Newton, et al.
Pageof 7

Showing results (31-40 of 66) with videos related to

Sort By:
Pageof 7
Biochemistry|April 19, 1994
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene productL Zheng, R H White, V L Cash, et al.
Journal of Inorganic Biochemistry|September 23, 2000
The role of the MoFe protein alpha-125Phe and beta-125Phe residues in Azotobacter vinelandii MoFe protein-Fe protein interactionJ Christiansen, J M Chan, L C Seefeldt, et al.
The Journal of Biological Chemistry|February 7, 2001
Isolation and characterization of an acetylene-resistant nitrogenaseJ Christiansen, V L Cash, L C Seefeldt, et al.
Biochemistry|June 14, 2000
Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysisJ M Chan, W Wu, D R Dean, et al.
Biochemistry|August 12, 1998
Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenaseW N Lanzilotta, J Christiansen, D R Dean, et al.
The Journal of Biological Chemistry|November 10, 1995
Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe proteinJ W Peters, K Fisher, W E Newton, et al.
The Journal of Biological Chemistry|May 28, 1998
Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandiiL Zheng, V L Cash, D H Flint, et al.
The Journal of Biological Chemistry|March 3, 1995
Characteristics of NIFNE in Azotobacter vinelandii strains. Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenaseJ T Roll, V K Shah, D R Dean, et al.
The Journal of Biological Chemistry|April 5, 1992
Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interactionL C Seefeldt, T V Morgan, D R Dean, et al.
Journal of Bacteriology|April 1, 1987
Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifKK E Brigle, M C Weiss, W E Newton, et al.
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