Ormö M - Search Results

1

Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein.

Brejc K, Sixma TK, Kitts PA, Kain SR, Tsien RY, Ormö M, Remington SJ. Brejc K, et al. Among authors: ormo m. Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2306-11. doi: 10.1073/pnas.94.6.2306. Proc Natl Acad Sci U S A. 1997. PMID: 9122190 Free PMC article.

2

Crystal structure of the Aequorea victoria green fluorescent protein.

Ormö M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Ormö M, et al. Science. 1996 Sep 6;273(5280):1392-5. doi: 10.1126/science.273.5280.1392. Science. 1996. PMID: 8703075

3

Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate.

Ormö M, Bystrom CE, Remington SJ. Ormö M, et al. Biochemistry. 1998 Nov 24;37(47):16565-72. doi: 10.1021/bi981616s. Biochemistry. 1998. PMID: 9843423

4

The conserved serine 211 is essential for reduction of the dinuclear iron center in protein R2 of Escherichia coli ribonucleotide reductase.

Regnström K, Aberg A, Ormö M, Sahlin M, Sjöberg BM. Regnström K, et al. Among authors: ormo m. J Biol Chem. 1994 Mar 4;269(9):6355-61. J Biol Chem. 1994. PMID: 8119985 Free article.

5

Autocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 protein.

Aberg A, Ormö M, Nordlund P, Sjöberg BM. Aberg A, et al. Among authors: ormo m. Biochemistry. 1993 Sep 21;32(37):9845-50. doi: 10.1021/bi00088a040. Biochemistry. 1993. PMID: 8373782

The mutant form Phe-208-->Tyr of the R2 protein of Escherichia coli ribonucleotide reductase contains an intrinsic ferric-Dopa cofactor with characteristic absorption bands at 460 and ca. 700 nm [Ormo, M., de Mare, F., Regnstrom, K., Aberg, A., Sahlin, M., …

The mutant form Phe-208-->Tyr of the R2 protein of Escherichia coli ribonucleotide reductase contains an intrinsic ferric-Dopa cofactor w …

6

The Cys292-->Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site.

Ormö M, Sjöberg BM. Ormö M, et al. Eur J Biochem. 1996 Oct 15;241(2):363-7. doi: 10.1111/j.1432-1033.1996.00363.x. Eur J Biochem. 1996. PMID: 8917431 Free article.

7

Residues important for radical stability in ribonucleotide reductase from Escherichia coli.

Ormö M, Regnström K, Wang Z, Que L Jr, Sahlin M, Sjöberg BM. Ormö M, et al. J Biol Chem. 1995 Mar 24;270(12):6570-6. doi: 10.1074/jbc.270.12.6570. J Biol Chem. 1995. PMID: 7896794 Free article.

8

Engineering of the iron site in ribonucleotide reductase to a self-hydroxylating monooxygenase.

Ormö M, deMaré F, Regnström K, Aberg A, Sahlin M, Ling J, Loehr TM, Sanders-Loehr J, Sjöberg BM. Ormö M, et al. J Biol Chem. 1992 May 5;267(13):8711-4. J Biol Chem. 1992. PMID: 1577712 Free article.

9

An ultrafiltration assay for nucleotide binding to ribonucleotide reductase.

Ormö M, Sjöberg BM. Ormö M, et al. Anal Biochem. 1990 Aug 15;189(1):138-41. doi: 10.1016/0003-2697(90)90059-i. Anal Biochem. 1990. PMID: 2278383

10

Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.

Aberg A, Hahne S, Karlsson M, Larsson A, Ormö M, Ahgren A, Sjöberg BM. Aberg A, et al. Among authors: ormo m. J Biol Chem. 1989 Jul 25;264(21):12249-52. J Biol Chem. 1989. PMID: 2663852 Free article.

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