B
B.H. Huynh
Researcher at Emory University
Publications - 32
Citations - 2288
B.H. Huynh is an academic researcher from Emory University. The author has contributed to research in topics: Hydrogenase & Desulfovibrio gigas. The author has an hindex of 23, co-authored 32 publications receiving 2227 citations. Previous affiliations of B.H. Huynh include University of Minnesota.
Papers
More filters
Journal ArticleDOI
The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio
G. Fauque,Harry D. Peck,José J. G. Moura,B.H. Huynh,Yves Berlier,Daniel V. DerVartanian,Miguel Teixeira,Alan Przybyla,Paul A. Lespinat,Isabel Moura,Jean LeGall +10 more
TL;DR: Three types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus Desulfovibrio and it is suggested that selenium is a ligand to nickel and suggest that the redox active nickel is ligated by at least two cysteinyl thiolate and one selenocysteine selenolate residues.
Journal ArticleDOI
On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments.
Journal ArticleDOI
Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies.
TL;DR: The tetrameric form of a Desulfovibrio gigas ferredoxin, named Fd II, mediates electron transfer between cytochrome c3 and sulfite reductase and the Mössbauer data demonstrate conclusively the presence of a spin-coupled structure containing 3 iron atoms and labile sulfur.
Journal ArticleDOI
Redox intermediates of Desulfovibrio gigas [NiFe] hydrogenase generated under hydrogen. Mössbauer and EPR characterization of the metal centers.
Miguel Teixeira,Isabel Moura,António V. Xavier,José J. G. Moura,Jean LeGall,Daniel V. DerVartanian,Harry D. Peck,B.H. Huynh +7 more
TL;DR: Detailed redox profiles for the previously reported Ni-signal C and the g = 2.21 signal were obtained in this study, and evidence was found to indicate that these two signals represent two different oxidation states of the enzyme.