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Literature summary for 7.1.1.9 extracted from

  • Lee, A.; Kirichenko, A.; Vygodina, T.; Siletsky, S.A.; Das, T.K.; Rousseau, D.L.; Gennis, R.; Konstantinov, A.A.
    Ca2+-binding site in Rhodobacter sphaeroides cytochrome c oxidase (2002), Biochemistry, 41, 8886-8898.
    View publication on PubMed
Search for more literature for 7.1.1.9

Protein Variants

Protein Variants Comment Organism
D485A mutant enzyme is active, binds to Ca2+ reversibly, and exhibits the red shift in the heme a absorption spectrum upon Ca2+ binding for both reduced and oxidized states of heme a. Sodium ions reverse the Ca2+-induced red shift of heme a and dramatically decrease the rate of Ca2+ binding to the mutant enzyme. With the mutant enzyme, 1 Ca2+ competes with 1 Na+ for the binding site Cereibacter sphaeroides
E54A/D485A inactive mutant enzyme does not assemble normally Cereibacter sphaeroides
E54L inactive mutant enzyme does not assemble normally Cereibacter sphaeroides
E54L/D485A/Q61L inactive mutant enzyme does not assemble normally Cereibacter sphaeroides
E54L/Q61L inactive mutant enzyme does not assemble normally Cereibacter sphaeroides
Q61A mutant enzyme is active and retains tighly bound Ca2+ Cereibacter sphaeroides
Q61L mutant enzyme is active and retains tighly bound Ca2+ Cereibacter sphaeroides

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ contains one Ca2+ per enzyme, tighly bound Ca2+ plays a structural role in the enzyme. Mutant enzyme D485A is active, binds to Ca2+ reversibly, and exhibits the red shift in the heme a absorption spectrum upon Ca2+ binding for both reduced and oxidized states of heme a. Sodium ions reverse the Ca2+-induced red shift of heme a and dramatically decrease the rate of Ca2+ binding to the mutant enzyme. With the mutant enzyme, 1 Ca2+ competes with 1 Na+ for the binding site Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
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