Search Results - "Jensen, Lyndal M.R"

In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex by Jensen, Lyndal M.R, Sanishvili, Ruslan, Davidson, Victor L, Wilmot, Carrie M

“…MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor…”
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Water-soluble scorpionate ligands and their reactions with molybdenum complexes. Crystal structures of lithium tris(3-isopropylpyrazol-1-yl)methanesulfonate and MoVOCl3(OPPh3)2·MoVIO2Cl2(OPPh3)2 by Jensen, Lyndal M.R., Abrahams, Brendan F., Young, Charles G.

“…The water soluble ligands, lithium and potassium tris(3-isopropylpyrazol-1-yl)methanesulfonate (LiTpms i Pr and KTpms i Pr ) and potassium…”
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Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis by Tarboush, Nafez Abu, Jensen, Lyndal M. R, Yukl, Erik T, Geng, Jiafeng, Liu, Aimin, Wilmot, Carrie M, Davidson, Victor L

“…The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of…”
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Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis by Yukl, Erik T., Liu, Fange, Krzystek, J., Shin, Sooim, Jensen, Lyndal M. R., Davidson, Victor L., Wilmot, Carrie M., Liu, Aimin

“…Despite the importance of tryptophan (Trp) radicals in biology, very few radicals have been trapped and characterized in a physiologically meaningful context…”
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Functional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine by Abu Tarboush, Nafez, Jensen, Lyndal M. R, Feng, Manliang, Tachikawa, Hiroyasu, Wilmot, Carrie M, Davidson, Victor L

“…The diheme enzyme MauG catalyzes the posttranslational modification of a precursor protein of methylamine dehydrogenase (preMADH) to complete the biosynthesis…”
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Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauG by Feng, Manliang, Jensen, Lyndal M. R, Yukl, Erik T, Wei, Xiaoxi, Liu, Aimin, Wilmot, Carrie M, Davidson, Victor L

“…The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to…”
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Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG by Jensen, Lyndal M. R., Meharenna, Yergalem T., Davidson, Victor L., Poulos, Thomas L., Hedman, Britt, Wilmot, Carrie M., Sarangi, Ritimukta

“…Biosynthesis of the tryptophan tryptophylquinone (TTQ) cofactor activates the enzyme methylamine dehydrogenase. The diheme enzyme MauG catalyzes O-atom…”
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Water-soluble scorpionate ligands and their reactions with molybdenum complexes. Crystal structures of lithium tris(3-isopropylpyrazol-1-yl)methanesulfonate and Mo V OCl 3 (OPPh 3 ) 2 ·Mo VI O 2 Cl 2 (OPPh 3 ) 2 by Jensen, Lyndal M.R., Abrahams, Brendan F., Young, Charles G.

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A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis by Abu Tarboush, Nafez, Jensen, Lyndal M.R., Wilmot, Carrie M., Davidson, Victor L.

“…•A W199E MauG mutation alters hydrogen bonding interactions with preMADH.•A W199E MauG mutation alters the kinetic mechanism of interprotein electron…”
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The Tightly Bound Calcium of MauG Is Required for Tryptophan Tryptophylquinone Cofactor Biosynthesis by Shin, Sooim, Feng, Manliang, Chen, Yan, Jensen, Lyndal M. R, Tachikawa, Hiroyasu, Wilmot, Carrie M, Liu, Aimin, Davidson, Victor L

“…The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to…”
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Structures of MauG in complex with quinol and quinone MADH by Yukl, Erik T., Jensen, Lyndal M. R., Davidson, Victor L., Wilmot, Carrie M.

“…MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o‐quinol (TTQOQ) and quinone (TTQOX) forms and the structures…”
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