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Science 7 October 1994:
Vol. 266. no. 5182, pp. 110 - 114
DOI: 10.1126/science.7939628
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Articles

Science, Vol 266, Issue 5182, 110-114
Copyright © 1994 by American Association for the Advancement of Science

articles

The mobile flavin of 4-OH benzoate hydroxylase

DL Gatti, BA Palfey, MS Lah, B Entsch, V Massey, DP Ballou, and ML Ludwig

Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.

Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.


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