Boi Hanh Huynh

发表

Diiron-cluster intermediates in biological oxygen activation reactions

D. Edmondson, B. Huynh, Dale E. Edmondson, 1996 .

{Generation of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly}

Carsten Krebs, Stephen J. Lippard, S. Lippard, 1998 .

Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath)

Stephen J. Lippard, S. Lippard, D. Edmondson, 1995 .

Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein.

D. Dean, M. Unciuleac, S. Naik, 2007, Biochemistry.

Reconsideration of X, the Diiron Intermediate Formed during Cofactor Assembly in E. coli Ribonucleotide Reductase

JoAnne Stubbe, J. Stubbe, B. Hoffman, 1996 .

Valence-Delocalized Diiron(II,III) Cores Supported by Carboxylate-Only Bridging Ligands

Carsten Krebs, Stephen J. Lippard, S. Lippard, 2000 .

Engineering the Diiron Site of Escherichia coli Ribonucleotide Reductase Protein R2 to Accumulate an Intermediate Similar to Hperoxo, the Putative Peroxodiiron(III) Complex from the Methane Monooxygenase Catalytic Cycle

Carsten Krebs, J. M. Bollinger, C. Krebs, 1998 .

Spectroscopic detection of intermediates in the reaction of dioxygen with the reduced methane monooxygenase/hydroxylase from Methylococcus capsulatus (Bath)

Athanasios Salifoglou, Stephen J. Lippard, S. Lippard, 1994 .

Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactor of E. Coli Ribonucleotide Reductase: 1. Moessbauer Characterization of the Diferric Radical Precursor

J. Martin Bollinger, Natarajan Ravi, JoAnne Stubbe, 1994 .