Literature summary for 1.8.2.1 extracted from

Rapson, T.D.; Kappler, U.; Hanson, G.R.; Bernhardt, P.V.
Short circuiting a sulfite oxidising enzyme with direct electrochemistry: active site substitutions and their effect on catalysis and electron transfer (2011), Biochim. Biophys. Acta, 1807, 108-118.

Search for more literature for 1.8.2.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Rhodobacter capsulatus	Starkeya novella

Protein Variants

Protein Variants	Comment	Organism
H57A	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent	Starkeya novella
R55K	heme potential is similar to wild-type, the molybdenum redox potential is not affected. Wild-type and mutant show pH dependence of the electrochemical catalytic halfwave potential	Starkeya novella
R55M	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent	Starkeya novella
R55Q	heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected	Starkeya novella

Organism

Organism	UniProt	Comment	Textmining
Starkeya novella	-	-	-

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Release 2023.1 (January 2023)