Loehr TM - Search Results

1

Resonance Raman studies of the stoichiometric catalytic turnover of a substrate-stearoyl-acyl carrier protein delta(9) desaturase complex.

Lyle KS, Möenne-Loccoz P, Ai J, Sanders-Loehr J, Loehr TM, Fox BG. Lyle KS, et al. Among authors: loehr tm. Biochemistry. 2000 Aug 29;39(34):10507-13. doi: 10.1021/bi000965v. Biochemistry. 2000. PMID: 10956041

2

Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins.

Fox BG, Shanklin J, Ai J, Loehr TM, Sanders-Loehr J. Fox BG, et al. Among authors: loehr tm. Biochemistry. 1994 Nov 1;33(43):12776-86. doi: 10.1021/bi00209a008. Biochemistry. 1994. PMID: 7947683

3

Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation.

Broadwater JA, Ai J, Loehr TM, Sanders-Loehr J, Fox BG. Broadwater JA, et al. Among authors: loehr tm. Biochemistry. 1998 Oct 20;37(42):14664-71. doi: 10.1021/bi981839i. Biochemistry. 1998. PMID: 9778341

4

Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy.

Sjöberg BM, Sanders-Loehr J, Loehr TM. Sjöberg BM, et al. Among authors: loehr tm. Biochemistry. 1987 Jul 14;26(14):4242-7. doi: 10.1021/bi00388a010. Biochemistry. 1987. PMID: 3311147

5

Raman spectral evidence for a mu-oxo bridge in the binuclear iron center of ribonucleotide reductase.

Sjöberg BM, Loehr TM, Sanders-Loehr J. Sjöberg BM, et al. Among authors: loehr tm. Biochemistry. 1982 Jan 5;21(1):96-102. doi: 10.1021/bi00530a017. Biochemistry. 1982. PMID: 7037052

6

Endothelial nitric oxide synthase: modulations of the distal heme site produced by progressive N-terminal deletions.

Rodríguez-Crespo I, Moënne-Loccoz P, Loehr TM, Ortiz de Montellano PR. Rodríguez-Crespo I, et al. Among authors: loehr tm. Biochemistry. 1997 Jul 15;36(28):8530-8. doi: 10.1021/bi970192j. Biochemistry. 1997. PMID: 9214298

7

O2 activation by non-heme diiron proteins: identification of a symmetric mu-1,2-peroxide in a mutant of ribonucleotide reductase.

Moënne-Loccoz P, Baldwin J, Ley BA, Loehr TM, Bollinger JM Jr. Moënne-Loccoz P, et al. Among authors: loehr tm. Biochemistry. 1998 Oct 20;37(42):14659-63. doi: 10.1021/bi981838q. Biochemistry. 1998. PMID: 9778340

8

The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O2-activating non-heme diiron proteins.

Moënne-Loccoz P, Krebs C, Herlihy K, Edmondson DE, Theil EC, Huynh BH, Loehr TM. Moënne-Loccoz P, et al. Among authors: loehr tm. Biochemistry. 1999 Apr 27;38(17):5290-5. doi: 10.1021/bi990095l. Biochemistry. 1999. PMID: 10220314

9

Formation of a bis(histidyl) heme iron complex in manganese peroxidase at high pH and restoration of the native enzyme structure by calcium.

Youngs HL, Moënne-Loccoz P, Loehr TM, Gold MH. Youngs HL, et al. Among authors: loehr tm. Biochemistry. 2000 Aug 15;39(32):9994-10000. doi: 10.1021/bi000679j. Biochemistry. 2000. PMID: 10933820

10

Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function.

Hirst J, Wilcox SK, Ai J, Moënne-Loccoz P, Loehr TM, Goodin DB. Hirst J, et al. Among authors: loehr tm. Biochemistry. 2001 Feb 6;40(5):1274-83. doi: 10.1021/bi002090q. Biochemistry. 2001. PMID: 11170453

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