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Literature summary for 1.2.7.4 extracted from

  • Tan, X.; Volbeda, A.; Fontecilla-Camps, J.C.; Lindahl, P.A.
    Function of the tunnel in acetylcoenzyme A synthase/carbon monoxide dehydrogenase (2006), J. Biol. Inorg. Chem., 11, 371-378.
    View publication on PubMed
Search for more literature for 1.2.7.4

Protein Variants

Protein Variants Comment Organism
A219F mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel Moorella thermoacetica
A578C mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel Moorella thermoacetica
F70W mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel Moorella thermoacetica
L215F mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel Moorella thermoacetica
N101Q mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel Moorella thermoacetica

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

Reaction

Reaction Comment Organism Reaction ID
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+ CO and CO2 enter and exit the enzyme at the water channel along the betabeta subunit interface. CO either enters the enzyme and migrates through the tunnel before binding at the A-cluster, or it binds the A-cluster directly from solvent Moorella thermoacetica
a