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Xianghui Li, Ph.D.

Affiliations: 
2008 The University of Mississippi Medical Center, Jackson, MS, United States 
Area:
Biochemistry
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"Xianghui Li"
Mean distance: 9953.25
 
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Victor L. Davidson grad student 2008 University of Mississippi Medical Center
 (Biosynthesis of the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase in vitro.)

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Chen F, Zhang G, Yu L, et al. (2016) High-efficiency generation of induced pluripotent mesenchymal stem cells from human dermal fibroblasts using recombinant proteins. Stem Cell Research & Therapy. 7: 99
Dey M, Li X, Kunz RC, et al. (2010) Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue. Biochemistry. 49: 10902-11
Dey M, Li X, Zhou Y, et al. (2010) Evidence for organometallic intermediates in bacterial methane formation involving the nickel coenzyme F₄₃₀. Metal Ions in Life Sciences. 7: 71-110
Li X, Telser J, Kunz RC, et al. (2010) Observation of organometallic and radical intermediates formed during the reaction of methyl-coenzyme M reductase with bromoethanesulfonate. Biochemistry. 49: 6866-76
Lee S, Shin S, Li X, et al. (2009) Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 48: 2442-7
Li X, Fu R, Lee S, et al. (2008) A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical. Proceedings of the National Academy of Sciences of the United States of America. 105: 8597-600
Li X, Fu R, Liu A, et al. (2008) Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry. 47: 2908-12
Li X, Jones LH, Pearson AR, et al. (2006) Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 13276-83
Pearson AR, Marimanikkuppam S, Li X, et al. (2006) Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase. Journal of the American Chemical Society. 128: 12416-7
Li X, Feng M, Wang Y, et al. (2006) Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 821-8
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