Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.
Open Access
- 1 December 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (35) , 25181-25188
- https://doi.org/10.1016/s0021-9258(19)74022-8
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Convergent evolution of similar function in two structurally divergent enzymesNature, 1991
- X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniquesJournal of Molecular Biology, 1989
- THIOREDOXINAnnual Review of Biochemistry, 1985
- The structure of the flavoenzyme glutathione reductaseNature, 1978
- Light-mediated reduction of flavoproteins with flavins as catalystsBiochemistry, 1978
- Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Appendix: photochemical formation of deazaflavin dimersBiochemistry, 1978
- Structure of the semiquinone form of flavodoxin from Clostridium MPJournal of Molecular Biology, 1977
- A photochemical procedure for reduction of oxidation-reduction proteins employing deazariboflavin as catalyst.Journal of Biological Chemistry, 1977
- Lone pair-lone pair interactions in unsymmetrical systems: RSSR vs. RSORJournal of the American Chemical Society, 1977
- Studies on Thioredoxin Reductase from Escherichia coli B. The Relation of Structure and FunctionEuropean Journal of Biochemistry, 1968