EC Number |
Cofactor |
Reference |
---|
2.8.4.1 | coenzyme F430 |
- |
738676 |
2.8.4.1 | coenzyme F430 |
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme |
673602 |
2.8.4.1 | coenzyme F430 |
a redox-active nickel tetrahydrocorphin bound at the active site, contains low-spin Ni(II), determination of the cofactor reduction site at the exocyclic ketone group by NMR study, mass spectrometry, and QM/MM computations, conversion of F430 to F330 reduces the hydrocorphin ring but not the metal, reduction of F430 with Ti(III) citrate to generate F380, corresponding to the active MCRred1 state, reduces the Ni(II) to Ni(I) but does not reduce the tetrapyrrole ring system, overview |
672069 |
2.8.4.1 | coenzyme F430 |
an essential redox-active nickel tetrahydrocorphin, bound at the active site, the active form of MCR, MCRred1, contains Ni(I)-F430 |
672222 |
2.8.4.1 | coenzyme F430 |
each active site has the nickel porphyrinoid F430 as a prosthetic group, in the active state, F430 contains the transition metal in the Ni(I) oxidation state |
674934 |
2.8.4.1 | coenzyme F430 |
structure analysis using crystal structure PDB code 1MRO, and conformational changes during catalysis, free cofactor F430 is thermally unstable, it first epimerizes to 13-epi F430 and then in a second epimerization to 12,13-diepi F430, nonplanar deformations, overview |
674001 |
2.8.4.1 | coenzyme F430 |
the nickel-containing tetrapyrrole is essential for the reaction, and is bound to the active site |
674693 |
2.8.4.1 | F-430 |
- |
393245, 393246, 393249, 393257, 661554, 725201 |
2.8.4.1 | F-430 |
1 mol coenzyme F-430/mol enzyme |
393251 |
2.8.4.1 | F-430 |
1.6-1.8 mol F-430/mol enzyme |
393256 |