B
Boi Hanh Huynh
Researcher at University of Georgia
Publications - 37
Citations - 2971
Boi Hanh Huynh is an academic researcher from University of Georgia. The author has contributed to research in topics: Ribonucleotide reductase & Ferric. The author has an hindex of 28, co-authored 37 publications receiving 2845 citations. Previous affiliations of Boi Hanh Huynh include Universidade Nova de Lisboa & North Carolina State University.
Papers
More filters
Journal ArticleDOI
IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.
Jeffrey N. Agar,Carsten Krebs,Jeverson Frazzon,Boi Hanh Huynh,Dennis R. Dean,Michael K. Johnson +5 more
TL;DR: The ability to assemble both [2Fe-2S](2+) and [4Fe-4S]-2+) clusters in IscU supports the proposal that this ubiquitous protein provides a scaffold for IscS-mediated assembly of clusters that are subsequently used for maturation of apo Fe-S proteins.
Journal ArticleDOI
IscA, an Alternate Scaffold for Fe−S Cluster Biosynthesis†
Carsten Krebs,Jeffrey N. Agar,Archer D. Smith,Jeverson Frazzon,Dennis R. Dean,Boi Hanh Huynh,Michael K. Johnson +6 more
TL;DR: It is proposed that the IscA family of proteins provide alternative scaffolds to the NifU and IscU proteins for mediating nif-specific and general Fe-S cluster assembly.
Journal ArticleDOI
Formation and Properties of [4Fe-4S] Clusters on the IscU Scaffold Protein†
Kala Chandramouli,Mihaela-Carmen Unciuleac,Sunil Naik,Dennis R. Dean,Boi Hanh Huynh,Michael K. Johnson +5 more
TL;DR: The results suggest that reductive coupling of adjacent [2Fe-2S]2+ clusters assembled on IscU provides a general mechanism for the final step in the biosynthesis of [4Fe-4S]3+ clusters, which may provide an effective way to populate appropriately cluster-loaded forms of Isc U for maturation of different types of [Fe-S] proteins.
Journal ArticleDOI
Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization
Alice S. Pereira,William C. Small,Carsten Krebs,Pedro Tavares,Dale E. Edmondson,Elizabeth C. Theil,Boi Hanh Huynh +6 more
TL;DR: The proposal that a single protein site, with a structure homologous to the diiron centers in MMOH and R2, is involved in the ferritin ferroxidation step is confirmed by the observed kinetics, spectroscopic properties, and purity of the initial peroxodiferric species formed in the frog M ferritIn.
Journal ArticleDOI
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study.
TL;DR: A dual-iron-isotope (56Fe/57Fe) approach is employed to demonstrate the existence of a unique Fe site in the [4Fe-4S] cluster of PFL-AE by Mössbauer spectroscopy, indicating that AdoMet coordination is a necessary prerequisite to adenosyl radical generation.