Haaker H - Search Results

1

On the prosthetic group(s) of component II from nitrogenase. EPR of the Fe-protein from Azotobacter vinelandii.

Hagen WR, Dunham WR, Braaksma A, Haaker H. Hagen WR, et al. Among authors: haaker h. FEBS Lett. 1985 Jul 22;187(1):146-50. doi: 10.1016/0014-5793(85)81231-x. FEBS Lett. 1985. PMID: 2991004 Free article.

2

A novel S = 3/2 EPR signal associated with native Fe-proteins of nitrogenase.

Hagen WR, Eady RR, Dunham WR, Haaker H. Hagen WR, et al. Among authors: haaker h. FEBS Lett. 1985 Sep 23;189(2):250-4. doi: 10.1016/0014-5793(85)81033-4. FEBS Lett. 1985. PMID: 2995120 Free article.

3

Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase.

Spee JH, Arendsen AF, Wassink H, Marritt SJ, Hagen WR, Haaker H. Spee JH, et al. Among authors: haaker h. FEBS Lett. 1998 Jul 31;432(1-2):55-8. doi: 10.1016/s0014-5793(98)00827-8. FEBS Lett. 1998. PMID: 9710250 Free article.

4

The importance of quantitative Mössbauer spectroscopy of MoFe-protein from Azotobacter vinelandii.

Dunham WR, Hagen WR, Braaksma A, Grande HJ, Haaker H. Dunham WR, et al. Among authors: haaker h. Eur J Biochem. 1985 Feb 1;146(3):497-501. doi: 10.1111/j.1432-1033.1985.tb08679.x. Eur J Biochem. 1985. PMID: 3855748 Free article.

5

The effect of the redox potential on the activity of the nitrogenase and on the Fe-protein of Azotobacter vinelandii.

Braaksma A, Haaker H, Grande HJ, Veeger C. Braaksma A, et al. Among authors: haaker h. Eur J Biochem. 1982 Jan;121(3):483-91. doi: 10.1111/j.1432-1033.1982.tb05813.x. Eur J Biochem. 1982. PMID: 6276174 Free article. No abstract available.

6

Fully active Fe-protein of the nitrogenase from Azotobacter vinelandii contains at least eight iron atoms and eight sulphide atoms per molecule.

Braaksma A, Haaker H, Veeger C. Braaksma A, et al. Among authors: haaker h. Eur J Biochem. 1983 Jun 1;133(1):71-6. doi: 10.1111/j.1432-1033.1983.tb07430.x. Eur J Biochem. 1983. PMID: 6574018 Free article.

7

Redox properties and EPR spectroscopy of the P clusters of Azotobacter vinelandii MoFe protein.

Pierik AJ, Wassink H, Haaker H, Hagen WR. Pierik AJ, et al. Among authors: haaker h. Eur J Biochem. 1993 Feb 15;212(1):51-61. doi: 10.1111/j.1432-1033.1993.tb17632.x. Eur J Biochem. 1993. PMID: 8383042 Free article.

8

Quantitative EPR of an S = 7/2 system in thionine-oxidized MoFe proteins of nitrogenase. A redefinition of the P-cluster concept.

Hagen WR, Wassink H, Eady RR, Smith BE, Haaker H. Hagen WR, et al. Among authors: haaker h. Eur J Biochem. 1987 Dec 15;169(3):457-65. doi: 10.1111/j.1432-1033.1987.tb13633.x. Eur J Biochem. 1987. PMID: 2826146 Free article.

9

Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands.

Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Hagen WR, et al. Among authors: haaker h. J Biol Inorg Chem. 2000 Aug;5(4):527-34. doi: 10.1007/pl00021452. J Biol Inorg Chem. 2000. PMID: 10968624

10

Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase.

Duyvis MG, Wassink H, Haaker H. Duyvis MG, et al. Among authors: haaker h. FEBS Lett. 1996 Feb 19;380(3):233-6. doi: 10.1016/0014-5793(96)00019-1. FEBS Lett. 1996. PMID: 8601431 Free article.

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