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Entry M0320    1.8.5.-    sulfide:quinone oxidoreductase

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Step 04

Ubiquinone, the physiological electron acceptor accepts a hydride from reduced FAD, regenerating the cofactor for the next round of sulfide oxidiation.

GIF of Reaction Step M0320.stg04


Comment: While potential proton donors to the ubiquinone identified in Acidithiobacillus ferrooxidans are conserved in the Acidianus ambivalens homolouge listed here, no general base to the FAD cofactor has been suggested in either case [3]. The reprotonation of Lys386 has been inferred.



Mechanisms

Hydride Transfer
Proton Transfer

Mechanism Components

Bond Cleavage
Bond Formation
Bond Order Change
Overall Reactant Used
Overall Product Formed
Cofactor Regenerated

Amino acids involved in the reaction step.

Amino Acid Location of Function Activity Function
Asp215A Side Chain spectator Hydrogen Bond Acceptor
Cys350A Side Chain spectator Covalently Attached
Cys178A Side Chain spectator Covalently Attached
Asp353A Side Chain spectator Hydrogen Bond Donor
Lys386A Side Chain reactant Activator
Proton Donor
Cys129A Side Chain spectator Covalently Attached

Organic Cofactors involved in the reaction step

Cofactor Type Cofactor Activity Function
FAD FAD401A reactant Activator
Proton Donor
Hydride Donor

Reactive Centre

Bonds Formed Bonds Cleaved Bonds Changed in Order Atom Types Involved
N-H
O-H
O-H
R-H
N-H
N-H
N-H
O-H
O-H
The C-C bond changes from a single to double bond
The C-C bond changes from a single to double bond
The C-N bond changes from a single to double bond
The C-N bond changes from a single to double bond
The C-C bond changes from a double to single bond
The C-C bond changes from a double to single bond
The C-O bond changes from a double to single bond
The C-O bond changes from a double to single bond
C
H
N
O
R

View similar reactions in MACiE.


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