L
Lei V. Liu
Researcher at Stanford University
Publications - 28
Citations - 1690
Lei V. Liu is an academic researcher from Stanford University. The author has contributed to research in topics: Nuclear resonance vibrational spectroscopy & Carbon nanotube. The author has an hindex of 20, co-authored 28 publications receiving 1520 citations. Previous affiliations of Lei V. Liu include University of British Columbia & Daegu Gyeongbuk Institute of Science and Technology.
Papers
More filters
Journal ArticleDOI
Structure and reactivity of a mononuclear non-haem iron( III )–peroxo complex
Jaeheung Cho,Sujin Jeon,Samuel A. Wilson,Lei V. Liu,Eun A. Kang,Joseph J. Braymer,Mi Hee Lim,Britt Hedman,Keith O. Hodgson,Joan Selverstone Valentine,Joan Selverstone Valentine,Edward I. Solomon,Wonwoo Nam +12 more
TL;DR: Reactivity results demonstrate that iron(iii)–hydroperoxo species are viable oxidants in both nucleophilic and electrophilic reactions by iron-containing enzymes.
Journal ArticleDOI
Elucidation of the Fe( iv )=O intermediate in the catalytic cycle of the halogenase SyrB2
Shaun D. Wong,Martin Srnec,Megan L. Matthews,Megan L. Matthews,Lei V. Liu,Yeonju Kwak,Kiyoung Park,Caleb B. Bell,E. Ercan Alp,Jiyong Zhao,Yoshitaka Yoda,Shinji Kitao,Makoto Seto,Carsten Krebs,J. Martin Bollinger,Edward I. Solomon,Edward I. Solomon +16 more
TL;DR: NRVS structural characterization of the reactive Fe(iv)=O intermediate of a NHFe enzyme, namely the halogenase SyrB2 from the bacterium Pseudomonas syringae pv.
Journal ArticleDOI
Chemistry of Single-Walled Carbon Nanotubes
Journal ArticleDOI
Geometric and Electronic Structure Contributions to Function in Non-heme Iron Enzymes
TL;DR: This methodology has developed a methodology that provides detailed geometric and electronic structure insights into these NHFe(II) active sites and defined a general mechanistic strategy that many of these enzymes use: they control O2 activation (and limit autoxidation and self-hydroxylation) by allowing Fe( II) coordination unsaturation only in the presence of cosubstrates.
Journal ArticleDOI
Peroxo and oxo intermediates in mononuclear nonheme iron enzymes and related active sites.
TL;DR: Current Opinion uses spectroscopy combined with electronic structure calculations to define the frontier molecular orbitals (FMOs) of Fe(III)OOH and Fe(IV)O intermediates and shows that the reactivity of this nonheme iron intermediate is very different from that of the analogous Compound 0 of cytochrome P450.