Literature summary for 1.8.2.2 extracted from

Kurth, J.M.; Brito, J.A.; Reuter, J.; Flegler, A.; Koch, T.; Franke, T.; Klein, E.M.; Rowe, S.F.; Butt, J.N.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase (2016), J. Biol. Chem., 291, 24804-24818.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3	Allochromatium vinosum

Organism

Organism	UniProt	Comment	Textmining
Allochromatium vinosum	D3RVD4	-	-

Synonyms

Synonyms	Comment	Organism
TsdA	-	Allochromatium vinosum

Cofactor

Cofactor	Comment	Organism	Structure
heme	reduction of His/Cys-ligated heme 1 occurs reversibly between approximately -100 and -350 mV. Reduction of His/Lys-ligated heme 2 is proposed to occur between approximately +150 and -100 mV	Allochromatium vinosum

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Release 2023.1 (January 2023)