scispace - formally typeset
J

Jean LeGall

Researcher at Universidade Nova de Lisboa

Publications -  14
Citations -  452

Jean LeGall is an academic researcher from Universidade Nova de Lisboa. The author has contributed to research in topics: Cytochrome & Electron paramagnetic resonance. The author has an hindex of 9, co-authored 14 publications receiving 437 citations. Previous affiliations of Jean LeGall include Louisiana State University.

Papers
More filters
Journal ArticleDOI

Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774)

TL;DR: Optical, electron paramagnetic resonance, and Mössbauer data of the gray desulfoferrodoxin indicate that both iron centers are in the high-spin ferric states, and resonance Raman studies confirm the structural similarity of center I and the distorted tetrahedral FeS4 center in desulforedoxin.
Journal ArticleDOI

Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp

TL;DR: A comparative study of electron transfer between the 16 heme high molecular mass cytochrome from Desulfovibrio vulgaris Hildenborough and the [Fe] and [NiFe] hydrogenases from the same organism indicates that the reduction of Hmc by the [ Fe] or [Ni Fe] hydrogenase is most likely mediated by cy tochrome c3.
Journal ArticleDOI

Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774)

TL;DR: A novel iron-sulfur protein was purified from the extract of Desulfovibrio desulfuricans to homogeneity as judged by polyacrylamide gel electrophoresis, providing direct spectroscopic evidence for the presence of a 6Fe cluster in this newly purified protein.
Journal ArticleDOI

Hexaheme nitrite reductase from Desulfovibrio desulfuricans. Mössbauer and EPR characterization of the heme groups.

TL;DR: Mössbauer and EPR spectroscopy were used to characterize the heme prosthetic groups of the nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774), which is a membrane-bound multiheme cytochrome capable of catalyzing the 6-electron reduction of nitrite to ammonia.