Entry M0105 188.8.131.52 aldehyde oxidase
Water deprotonates the thiolate group part of the Mo(V) coordination sphere, causing the elimination of Glu869 from the Mo(V) coordination sphere, and transfer of the second electron from Mo(V) to the acceptor via two iron-sulfur clusters.
It is unknown whether this reaction is reversible or not.
Comment: The overall arrangement of the metal centres in this enzyme is such that they are approximately linear, with Mo and the second 2Fe:2S cluster separated by approx 15 Angstroms, and the two 2Fe:2S clusters separated by approx 12 Angstroms. However, there are direct interactions between the metal centre ligands. The molybdopterin interacts directly with the second 2Fe:2S cluster through a H-bond formed between the N2 atom and the SG of the cluster ligand Cys139. The first and second 2Fe:2S clusters are further linked through a series of covalent and hydrogen bond interactions connecting the two cluster ligands Cys45 and Cys137. These interactions facilitate the electron transfer (which may occur through multiple steps) to an external electron acceptor . It should be noted that the exact atom in the iron sulfur cluster which is accepting the electron is unknown.
Amino acids involved in the reaction step.
||Location of Function
Metal Cofactors involved in Step 04
||Bonds Changed in Order
||Atom Types Involved
The Mo-S bond changes from a single to double bond
View similar reactions in MACiE.