Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774.
Paixão, Vitor B; Vis, Hans; Turner, David L.
; 49(44): 9620-9, 2010 Nov 09.
Artigo em Inglês | MEDLINE | ID: mdl-20886839
MetREx: a protein design approach for the exploration of sequence-reactivity relationships in metalloenzymes.
Electron transfer between periplasmic formate dehydrogenase and cytochromes c in Desulfovibrio desulfuricans ATCC 27774.
Desulfovibrio desulfuricans G20 tetraheme cytochrome structure at 1.5 Angstrom and cytochrome interaction with metal complexes.
The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.
Versatility of a new bioinorganic catalyst: palladized cells of Desulfovibrio desulfuricans and application to dehalogenation of flame retardant materials.
The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme.
Hydrogenase activity of mineral-associated and suspended populations of Desulfovibrio desulfuricans Essex 6.
Desulfovibrio desulfuricans isolates from the gut of a single individual: structural and biological lipid A characterization.
Genome sequence of the mercury-methylating strain Desulfovibrio desulfuricans ND132.