Seefeldt LC - Search Results

1

Mechanism of N₂ Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H₂.

Harris DF, Lukoyanov DA, Shaw S, Compton P, Tokmina-Lukaszewska M, Bothner B, Kelleher N, Dean DR, Hoffman BM, Seefeldt LC. Harris DF, et al. Among authors: seefeldt lc. Biochemistry. 2018 Feb 6;57(5):701-710. doi: 10.1021/acs.biochem.7b01142. Epub 2018 Jan 17. Biochemistry. 2018. PMID: 29283553 Free PMC article.

2

Kinetic and spectroscopic analysis of the inactivating effects of nitric oxide on the individual components of Azotobacter vinelandii nitrogenase.

Hyman MR, Seefeldt LC, Morgan TV, Arp DJ, Mortenson LE. Hyman MR, et al. Among authors: seefeldt lc. Biochemistry. 1992 Mar 24;31(11):2947-55. doi: 10.1021/bi00126a015. Biochemistry. 1992. PMID: 1312859

3

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 interaction.

Seefeldt LC, Morgan TV, Dean DR, Mortenson LE. Seefeldt LC, et al. J Biol Chem. 1992 Apr 5;267(10):6680-8. J Biol Chem. 1992. PMID: 1313018 Free article.

4

Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.

Lanzilotta WN, Holz RC, Seefeldt LC. Lanzilotta WN, et al. Among authors: seefeldt lc. Biochemistry. 1995 Dec 5;34(48):15646-53. doi: 10.1021/bi00048a007. Biochemistry. 1995. PMID: 7495793

5

Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129.

Lanzilotta WN, Ryle MJ, Seefeldt LC. Lanzilotta WN, et al. Among authors: seefeldt lc. Biochemistry. 1995 Aug 29;34(34):10713-23. doi: 10.1021/bi00034a003. Biochemistry. 1995. PMID: 7662655

6

Carbonyl sulfide and carbon dioxide as new substrates, and carbon disulfide as a new inhibitor, of nitrogenase.

Seefeldt LC, Rasche ME, Ensign SA. Seefeldt LC, et al. Biochemistry. 1995 Apr 25;34(16):5382-9. doi: 10.1021/bi00016a009. Biochemistry. 1995. PMID: 7727396

7

A continuous, spectrophotometric activity assay for nitrogenase using the reductant titanium(III) citrate.

Seefeldt LC, Ensign SA. Seefeldt LC, et al. Anal Biochem. 1994 Sep;221(2):379-86. doi: 10.1006/abio.1994.1429. Anal Biochem. 1994. PMID: 7810881

8

Circular dichroism and x-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form.

Ryle MJ, Lanzilotta WN, Seefeldt LC, Scarrow RC, Jensen GM. Ryle MJ, et al. Among authors: seefeldt lc. J Biol Chem. 1996 Jan 19;271(3):1551-7. doi: 10.1074/jbc.271.3.1551. J Biol Chem. 1996. PMID: 8576152 Free article.

9

Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineering.

Ryle MJ, Seefeldt LC. Ryle MJ, et al. Among authors: seefeldt lc. Biochemistry. 1996 Apr 16;35(15):4766-75. doi: 10.1021/bi960026w. Biochemistry. 1996. PMID: 8664266

10

Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complex.

Lanzilotta WN, Fisher K, Seefeldt LC. Lanzilotta WN, et al. Among authors: seefeldt lc. Biochemistry. 1996 Jun 4;35(22):7188-96. doi: 10.1021/bi9603985. Biochemistry. 1996. PMID: 8679547

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