Lipscomb JD - Search Results

1

Role of the nonheme Fe(II) center in the biosynthesis of the plant hormone ethylene.

Rocklin AM, Tierney DL, Kofman V, Brunhuber NM, Hoffman BM, Christoffersen RE, Reich NO, Lipscomb JD, Que L Jr. Rocklin AM, et al. Among authors: lipscomb jd. Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7905-9. doi: 10.1073/pnas.96.14.7905. Proc Natl Acad Sci U S A. 1999. PMID: 10393920 Free PMC article.

2

Mössbauer and EPR spectroscopy of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa.

Que L Jr, Lipscomb JD, Zimmermann R, Münck E, Orme-Johnson NR, Orme-Johnson WH. Que L Jr, et al. Among authors: lipscomb jd. Biochim Biophys Acta. 1976 Dec 8;452(2):320-34. doi: 10.1016/0005-2744(76)90182-0. Biochim Biophys Acta. 1976. PMID: 188463

3

Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications.

Que L Jr, Lipscomb JD, Münck E, Wood JM. Que L Jr, et al. Among authors: lipscomb jd. Biochim Biophys Acta. 1977 Nov 23;485(1):60-74. doi: 10.1016/0005-2744(77)90193-0. Biochim Biophys Acta. 1977. PMID: 199266

4

Resonance Raman studies of the protocatechuate 3,4-dioxygenase from Brevibacterium fuscum.

Siu DC, Orville AM, Lipscomb JD, Ohlendorf DH, Que L Jr. Siu DC, et al. Among authors: lipscomb jd. Biochemistry. 1992 Nov 3;31(43):10443-8. doi: 10.1021/bi00158a005. Biochemistry. 1992. PMID: 1420163

5

Gentisate 1,2-dioxygenase from pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans.

Harpel MR, Lipscomb JD. Harpel MR, et al. Among authors: lipscomb jd. J Biol Chem. 1990 Apr 15;265(11):6301-11. J Biol Chem. 1990. PMID: 2156846 Free article.

6

An EXAFS study of the interaction of substrate with the ferric active site of protocatechuate 3,4-dioxygenase.

True AE, Orville AM, Pearce LL, Lipscomb JD, Que L Jr. True AE, et al. Among authors: lipscomb jd. Biochemistry. 1990 Dec 4;29(48):10847-54. doi: 10.1021/bi00500a019. Biochemistry. 1990. PMID: 2271684

7

4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein.

Bradley FC, Lindstedt S, Lipscomb JD, Que L Jr, Roe AL, Rundgren M. Bradley FC, et al. Among authors: lipscomb jd. J Biol Chem. 1986 Sep 5;261(25):11693-6. J Biol Chem. 1986. PMID: 3017941 Free article.

8

X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism.

Shu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L Jr. Shu L, et al. Among authors: lipscomb jd. Biochemistry. 1995 May 23;34(20):6649-59. doi: 10.1021/bi00020a010. Biochemistry. 1995. PMID: 7756296

9

Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase.

Wolgel SA, Dege JE, Perkins-Olson PE, Jaurez-Garcia CH, Crawford RL, Münck E, Lipscomb JD. Wolgel SA, et al. Among authors: lipscomb jd. J Bacteriol. 1993 Jul;175(14):4414-26. doi: 10.1128/jb.175.14.4414-4426.1993. J Bacteriol. 1993. PMID: 8392511 Free PMC article.

10

Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity.

Miller MA, Lipscomb JD. Miller MA, et al. Among authors: lipscomb jd. J Biol Chem. 1996 Mar 8;271(10):5524-35. doi: 10.1074/jbc.271.10.5524. J Biol Chem. 1996. PMID: 8621411 Free article.

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