Penner-Hahn J - Search Results

1

Unexpected plasticity of the quaternary structure of iron-manganese superoxide dismutases.

Mendoza Rengifo E, Stelmastchuk Benassi Fontolan L, Ribamar Ferreira-Junior J, Bleicher L, Penner-Hahn J, Charles Garratt R. Mendoza Rengifo E, et al. Among authors: penner hahn j. J Struct Biol. 2022 Jun;214(2):107855. doi: 10.1016/j.jsb.2022.107855. Epub 2022 Apr 4. J Struct Biol. 2022. PMID: 35390463

2

X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase.

Tierney DL, Fee JA, Ludwig ML, Penner-Hahn JE. Tierney DL, et al. Biochemistry. 1995 Feb 7;34(5):1661-8. doi: 10.1021/bi00005a022. Biochemistry. 1995. PMID: 7849025

3

Manganese catalases.

Yoder DW, Hwang J, Penner-Hahn JE. Yoder DW, et al. Met Ions Biol Syst. 2000;37:527-57. Met Ions Biol Syst. 2000. PMID: 10693144 Review. No abstract available.

4

The interaction of mitochondrial iron with manganese superoxide dismutase.

Naranuntarat A, Jensen LT, Pazicni S, Penner-Hahn JE, Culotta VC. Naranuntarat A, et al. J Biol Chem. 2009 Aug 21;284(34):22633-40. doi: 10.1074/jbc.M109.026773. Epub 2009 Jun 27. J Biol Chem. 2009. PMID: 19561359 Free PMC article.

5

Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.

Mathieu E, Tolbert AE, Koebke KJ, Tard C, Iranzo O, Penner-Hahn JE, Policar C, Pecoraro V. Mathieu E, et al. Chemistry. 2020 Jan 2;26(1):249-258. doi: 10.1002/chem.201903808. Epub 2019 Dec 3. Chemistry. 2020. PMID: 31710732 Free PMC article.

6

The zinc coordination site of the bacteriophage Mu translational activator protein, Com.

Witkowski RT, Hattman S, Newman L, Clark K, Tierney DL, Penner-Hahn J, McLendon G. Witkowski RT, et al. J Mol Biol. 1995 Apr 7;247(4):753-64. doi: 10.1006/jmbi.1995.0178. J Mol Biol. 1995. PMID: 7723029 Free article.

7

Structure and dynamics of metalloproteins in live cells.

Cook JD, Penner-Hahn JE, Stemmler TL. Cook JD, et al. Methods Cell Biol. 2008;90:199-216. doi: 10.1016/S0091-679X(08)00810-8. Methods Cell Biol. 2008. PMID: 19195552 Free PMC article.

8

Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.

Hernick M, Gattis SG, Penner-Hahn JE, Fierke CA. Hernick M, et al. Biochemistry. 2010 Mar 16;49(10):2246-55. doi: 10.1021/bi902066t. Biochemistry. 2010. PMID: 20136146 Free PMC article.

9

Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity.

Koebke KJ, Yu F, Salerno E, Van Stappen C, Tebo AG, Penner-Hahn JE, Pecoraro VL. Koebke KJ, et al. Angew Chem Int Ed Engl. 2018 Apr 3;57(15):3954-3957. doi: 10.1002/anie.201712757. Epub 2018 Jan 26. Angew Chem Int Ed Engl. 2018. PMID: 29316146 Free PMC article.

10

Making or Breaking Metal-Dependent Catalytic Activity: The Role of Stammers in Designed Three-Stranded Coiled Coils.

Pinter TBJ, Manickas EC, Tolbert AE, Koebke KJ, Deb A, Penner-Hahn JE, Pecoraro VL. Pinter TBJ, et al. Angew Chem Int Ed Engl. 2020 Nov 9;59(46):20445-20449. doi: 10.1002/anie.202008356. Epub 2020 Sep 2. Angew Chem Int Ed Engl. 2020. PMID: 32748510 Free PMC article.

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